It is reasonable

It is reasonable selleckchem to suspect that modification of the PV microenvironment by additional secretion systems is also important in C. burnetii host cell parasitism. Gram-negative bacteria can employ several secretion systems to translocate proteins into the extracellular milieu [17]. However, bioinformatic analysis of the C. burnetii genome reveals canonical components of only a type I secretion system with the presence of a tolC homolog [18, 19]. Type I secretion is typically a one step process that transports proteins directly from the bacterial cytoplasm

into the surrounding environment [20]. However, a small number of proteins, such as heat-stable enterotoxins I and II of Nutlin-3a cost Escherichia coli[21, 22], and an ankyrin repeat protein of Rickettsia typhi[23], appear to access TolC via the periplasm after transport across the inner membrane by the Sec translocase. C. burnetii lacks typical constituents of a type II secretion system [24]. However, the organism encodes several genes involved in type IV pili (T4P) assembly, several of which are homologous to counterparts of type II secretion systems, indicating a common evolutionary

origin and possibly a similar function [25]. Accumulating data indicates core T4P proteins can constitute a secretion system [26–30]. In Francisella novicida, a collection of T4P proteins form a secretion system that Selleck PCI-32765 secretes at least 7 proteins [27]. In Vibrio cholerae, T4P secrete a soluble colonization factor required for optimal intestinal colonization of infant mice [30]. Dichelobacter nodosus secrete proteases in a T4P-dependent manner [29, 31]. Like the well-studied type II secretion system of Legionella pneumophila, a close phylogenetic relative of C. burnetii[18],

substrates secreted by T4P are biased towards N-terminal signal sequence-containing enzymes [27, 32]. C. burnetii encodes several enzymes with predicted signal Adenylyl cyclase sequences, such as an acid phosphatase (CBU0335) that inhibits neutrophil NADPH oxidase function and superoxide anion production [33, 34]. Along with PV detoxification, C. burnetii exoenzymes could presumably degrade macromolecules into simpler substrates that could then be transported by the organism’s numerous transporters [18]. Genome analysis indicates C. burnetii possesses a complete Sec translocase for translocation of signal sequence-containing proteins into the periplasm [18, 19]. Another secretion mechanism employed by Gram-negative bacteria is release of outer membrane vesicles (OMVs). OMVs capture periplasmic components before the vesicle pinches off from the cell envelope. This ‘packaging’ of proteins is thought to provide a protective environment for delivery of the contents. OMVs are implicated in a variety of functions including delivery of virulence factors, killing of competing bacteria, and suppression of host immune responses [35, 36]. The discovery of host cell-free growth of C.

Lancet Oncology 2005, 6:871–876 PubMedCrossRef 9 Goh KL, Quek KF

Lancet Oncology 2005, 6:871–876.PubMedCrossRef 9. Goh KL, Quek KF, Yeo GT, Hilmi IN, Lee CK, Hasnida N, Aznan M, Kwan KL, Ong KT: Colorectal Cancer in Asians; a demographic and anatomic survey

in Malaysian patients undergoing colonoscopy. Aliment Pharmacol Ther 2005, 22:859–864.PubMedCrossRef 10. Livak KJ, Schmittgen TD: Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2 -ΔΔC T Method. Methods 2001, 25:402–408.PubMedCrossRef 11. Smith RA, Cokkinides V, Brooks D, Saslow D, Brawley OW: Cancer Screening in the United States, 2010: A Review of Current American Cancer Society Guidelines and Issues in Cancer Screening. CA Cancer J Clin 2010, 60:99–119.PubMedCrossRef 12. Levin B, Lieberman Enzalutamide DA, McFarland BM, Smith RA, Brooks D, Andrews KS, Dash C, Giardiello FM, Glick S, Levin TR, Pickhardt P, Rex DK, Thonrson A, Winawer SJ: Screening and Surveillance

for the Early Detection Fludarabine mouse of Colorectal Cancer and Adenomatous Polyps, 2008: A Joint Guideline from the American Cancer Society, the US multi-Society Task Force on Colorectal Cancer, and the American College of Radiology. CA Cancer J Clin 2008, 58:130–160.PubMedCrossRef Competing interests David Suria, Chun Ren Lim, Choong Chin Liew and Guey Hooi Ng are employees of or consultants to GeneNews Ltd, who sponsored this research. Authors’ contributions DS and CRL drafted the manuscript. GHN carried out the RT-PCR and data analysis; KTY and PKD examined and diagnosed the patients, collected patient records, participated in the Everolimus nmr design of the study and critically reviewed the manuscript; CCL conceived the study and critically reviewed the manuscript. All authors have read and approved the final manuscript.”
“Background not Metastatic melanoma is a highly aggressive, often fatal malignancy, which exhibits resistance to all the current therapeutic approaches. At the time

of diagnosis, about 20% of melanoma patients already have metastatic disease. Once metastasis has occurred, the overall median survival is only 6-9 months [1]. The recent increase in the incidence of melanoma has brought to light the need for novel molecular approaches for treating melanoma metastasis [2]. Metastasis is a complex process that is dependent on the capacity of cancer cells to invade and migrate into adjoining cells and tissues, and proliferate into tumor growths [3, 4]. Consistent with this definition, cell invasion and migration are highly related to the activity of matrix metalloproteinases (MMPs) that regulate many processes involved in tumor evolution, such as cell growth, migration, and extracellular matrix (ECM) degradation [5]. Notably, MMP-1, MMP-2, MMP-9, and MMP-14 (MT1-MMP) have been implicated in the invasion and metastatic processes in several cancers [6, 7]. Cell adhesion is an essential process of metastatic cascades.

no Mass kDa pI MP Score SC % Cl no Profile Alpha-amylase, extr

no. Mass kDa pI MP Score SC % Cl. no. Profile Alpha-amylase, extracellular 6601 53 NCBInr

A2QL05 556 4.5 5 315 13 35 Fatty acid synthase subunit alpha 6465 764 Niraparib NCBInr A2Q7B6 205 5.9 10 387 5 35 Glucose-6-phosphate 1-dehydrogenase 6561 59 Swiss-Prot P48826 59 6.2 3 130 7 35 Glutamine synthetase 6714 42 NCBInr A2Q9R3 42 5.5 4 290 16 Selleckchem Saracatinib 4 Heat shock protein Hsp70 6481 73 NCBInr A2QPM8 70 5.1 5 198 12 4 Isocitrate dehydrogenase [NADP], mitochondrial, precursor 6644 48 Swiss-Prot P79089 56 8.5 8 339 14 19 NADP-dependent glutamate dehydrogenase 6647 48 NCBInr A2QHT6 50 5.8 6 382 18 4 Predicted 2-nitropropane dioxygenase 6737 41 NCBInr A2QKX9 386 5.7 4 112 17 35 Predicted glucose-methanol-choline (Gmc) oxidoreductase 6515 65 NCBInr A2R501 65 5.4 6 373 18 35 Predicted methyltransferase 6810 36 NCBInr A2QNF3 37 5.9 5 200 21 30 Predicted NADH cytochrome b5 reductase 6693 44 NCBInr A2R2Z2 46 5.4 6 530 20 4 Predicted ubiquitin conjugating enzyme 7044 17 NCBInr A2QDZ9 17 5.5 2 105 18 4 Putative 6-phosphogluconate dehydrogenase, decarboxylating 6660 47 NCBInr Q874Q3 PF299 price 55 5.9 9 527 27 35 Putative aconitate hydratase, mitochondrial

6472 75 NCBInr A2QSF4 84 6.2 7 278 11 35 Putative heat shock protein Ssc1, mitochondrial 6487 71 NCBInr A2R7X5 72 5.6 5 282 9 4 Putative histidine biosynthesis trifunctional protein 6413 1015 NCBInr A2QAS4 92 5.4 2 147 3 4 Putative inositol-1-phosphate synthase 6573 57 NCBInr A2QV05 58 5.7 2 62 4 35 Putative ketol-acid reductoisomerase, mitochondrial 6730 41 NCBInr A2QU08 456 8.9 8 467 17 35 Putative oxoglutarate dehydrogenase 6408 1015 NCBInr A2QIU5 119 6.3 10 349 8 35 Putative peroxiredoxin pmp20, peroxisomal membrane 7000 22 NCBInr A2R0G9 19 5.4 8 610 54 4 Putative peroxiredoxin Prx1, mitochondrial 6944 28 NCBInr A2QIF8 23 5.2 5 224 22 4 Putative pyruvate dehydrogenase E1 component subunit alpha, mitochondrial precurser 7028 184 NCBInr A2QPI1 45 7.6 2 160 7 30 Putative transaldolase 6787 38 NCBInr A2QMZ4 36 5.6 5 319 20 4 Putative transketolase 6471 75 NCBInr Q874Q5 75 6.0 6 246 11 4 Thioredoxin reductase 6680 45 NCBInr

A2Q9P0 39 5.2 6 449 22 4 Uncharacterised second protein 6965 26 NCBInr A2QDU1 19 5.4 3 147 15 4 Uncharacterised protein 6591 55 NCBInr A2QDX8 57 5.8 10 601 23 4 Uncharacterised protein 6592 55 NCBInr A2QDX8 57 5.8 10 717 25 4 Uncharacterised protein 7059 16 NCBInr A5ABN7 26 10.3 2 145 14 35 Uncharacterised protein 7092 135 NCBInr A2QSA8 13 5.2 2 249 35 4 List of identified proteins showing from left to right: Protein name, spot id and observed mass on gels, database, UniProt KB accession number, expected mass and isoelectric point (pI), number of matching peptide sequences (MP), Mowse Score (Score) and sequence coverage (SC), cluster and graph showing protein levels (average relative spot volume ± standard deviation) on media containing 3% starch (left/blue), 3% starch + 3% lactate (middle/purple) and 3% lactate (right/red).

The average telomere length was measured in all samples using the

The average telomere length was measured in all samples using the TeloTAGGG Telomere length Assay (Roche). Briefly, purified genomic DNA (6–8 μg) was digested by specific restriction enzymes. The DNA fragments were separated by gel electrophoresis and transferred to a nylon membrane using Southern

blotting. The blotted DNA fragments Doramapimod chemical structure were hybridized to a digoxigenin-labeled probe specific to telomere repeats and incubated with a digoxigenin-specific antibody coupled to alkaline phosphate. Finally, the immobilized probe was visualized by a sensitive chemiluminescence substrate and the average TRF length was assessed by comparing the signals relative to a molecular weight standard. Quantification of telomerase activity The telomeric repeats amplification protocol (TRAP)

was combined with real-time PLX-4720 detection of amplification products to determine telomerase activity using a Quantitative Telomerase Detection kit (US Biomax) following the manufacturer’s recommendations. Total protein extracts (0.5 μg) were used for each reaction. The end products were resolved by PAGE on a 12.5% non-denaturing gel, stained with Sybr Green Nucleic Acid gel stain (buy GDC-0973 Invitrogen) and visualized using the Bio-Rad Molecular Imager ChemiDoc System. Real-time quantitative reverse transcriptase-polymerase chain reaction (PCR) Each tissue sample was homogenized and total cellular RNA was extracted using the MasterPure Complete DNA and RNA Purification Kit (Epicentre) according to the manufacturer’s instructions. Before reverse transcription, RNA was treated with Methocarbamol DNase (Invitrogen-Life technology) to prevent DNA contamination. First-strand complementary DNA (cDNA) was synthesized from 0.5 μg RNA using random primers (Promega) and Superscript II reverse transcriptase (Invitrogen). The RNA concentration and purity were determined using a NanoDrop instrument (Thermo

Scientific). The primer sequences are available upon request. Primer sets used to quantify gene expression were first tested in PCR with a control cDNA to ensure specific amplification, as evidenced by the presence of a unique specific signal after agarose gel electrophoresis. PCR assays were performed on an ABI Prism 7000 sequence detection system (Applied Biosystems) using 5 μL of cDNA, 6 μL of SYBR Green Master Mix, 0.25 μL of ROX (Invitrogen) and 0.75 μL of primers at 10 μM. Thermal cycling consisted of a first cycle at 50°C for 2 min and 95°C for 10 min, followed by 40 cycles at 95°C for 15 seconds and 60°C for 1 min. Finally at the end of each PCR run, temperature was raised up to 95°C in order to check the melting curve.

The prototype nanofluidic device based on nanopores for single DN

The prototype nanofluidic device based on nanopores for single DNA sequencing

or biomolecular sensing; and the AFM image of PC nanopore arrays is showed in the top right corner. Although much progress has been achieved in nanopore techniques, it is still difficult to sense nucleotides at single-base resolution in DNA. That is mainly because the thickness of nanopores (about several nanometers) can permit 10 to 15 nucleotides occupying them at one time. On the other hand, the momentary change Avapritinib chemical structure in ionic currents is at only nano-ampere or pico-ampere level, and the duration of this change is at millisecond or so, which is hard to detect and analyzed. To improve the intensity of signals is an important selleck inhibitor issue in this area. Nanopore

arrays, which can be regarded as the integration of multiple nanochannels in the same direction, can improve the intensity of signals in ionic current changes compared to single pore. Now, nanopore arrays are widely used in biomolecular separation, detection and analysis, although it seems difficult for DNA sequencing at present. In this work, the single molecule translocation properties through polycarbonate nanopore arrays are studied and discussed. Methods Experimental device and reagent Polycarbonate membranes containing nanopore arrays (nanopore diameter 50 nm, nanopore distribution density 6 pores/μm2, thickness of polycarbonate membranes 6 to 11 μm) are purchased from the branch in China of Whatman, Inc. (Shanghai, China), and hydrophilic treatments are carried out before its usage. Goat antibody to human immunoglobulin

G (IgG) is imported from America Basic Gene Associate Bioscience, Inc. through Nanjing Boquan Technology Co., Ltd. (Nanjing, China). KCl is commercially available, and it is of analytical grade. Ultra-pure water (resistivity 18.25 MΩ·cm) is used for the preparation of all solutions and rinsing. CBL0137 concentration Keithley 2000 61/2-digital multimeter (Keithley Instruments selleck chemical Inc., Beijing, China) is used for ionic current recording. The applied voltage used in the experiments is varied 0.5 to 2V. AFM image in tapping mode is obtained from MFP-3D-SA atomic force microscope produced by Asylum Research (Santa Barbara, USA), and the scanning rate is 1.0 Hz. A test device (Figure 1) integrated by two separated liquid cells linked by PC membrane containing nanopore arrays (sealed by PDMS) is used for measuring ionic currents. At room temperature, KCl solution is added to the feed cell and permeation cell, and IgG is dissolved in the reservoir. After that, the electric field is applied to the two sides of the membrane, and the trans-membrane ionic current can be measured by Keithley 2000 61/2-digital multimeter and recorded simultaneously by computer. Simulation model A simple model is suggested to depict IgG molecules passing through nanopore arrays.

​genouest ​org/​) SOR genes were detected in the three kingdoms

​genouest.​org/​). SOR genes were detected in the three kingdoms of life, and only on chromosomal replicons. Although no N-terminal see more signal sequences were previously described for bacteria SOR [43], we predicted seven SOR to be potentially TAT-secreted (Twin-arginine translocation) in some bacteria, including for example in Desulfovibrio salexigens DSM 2638, Desulfuromonas acetoxidans DSM 684 and Geobacter uraniireducens Rf4. Our analysis confirms

the AP24534 observations by Pinto et al in 2010 that (1) the repartition of SOR classes does not correlate with organism phylogeny and that (2) sor genes occur in very diverse genetic environments. Indeed, although some sor are clustered with genes encoding electron donors

(such as rubredoxin in D. vulgaris) or inter-related oxidative responsive genes, most are close to functionally unrelated genes. This is consistent with sor genes being acquired, or lost, through lateral gene transfer [41]. Construction and content Collection of SOR For collection of SOR, we have extensively searched the Pubmed database and identified all relevant literature concerning any protein with “”superoxide reductase”" activity; this search resulted in a small learn more dataset (13 SOR published in 12 organisms, see Table 1). We therefore enriched the database using manually curated sequences described as desulfoferrodoxin (160 proteins), superoxide reductase (50 proteins) or neelaredoxin (9 proteins) in EntrezGene and/or GenBank entries. As the “”centre II”" is the Ketotifen active site for the SOR activity, we also included all proteins with a domain of this type as described in InterPro

(IPR002742, IPR004793, IPR004462, IPR012002), Pfam (PF01880, PF06397), Supfam (SSF49367), TIGRfam (TIGR00332, TIGR00320, TIGR00319), NCBI conserved domains (cd03172, cd03171, cd00524, cl00018, cl00014, cd00974) and PRODOM (PD006618, PD330262, PDA2O7Z7, PDA36750, PD985590, PDA36751, PDA63215, PDA7Y161, PDA7Y162, PD511041, PD171746, PD985589, PDA7Y163). All sequences collected were cleaned up to remove redundancy and unrelated proteins. This non-redundant and curated dataset was used to investigate the 1237 complete and 1345 in-draft genomes available in the NCBI database (May, 2010) through a series of successive BlastP [44] and tBlanstN [45] searches. Orthology (KO K05919 and COG2033) and synteny (IMG neighbourhood interface) were also exploited. To be as comprehensive as possible in the data collection, we performed multiple alignments using both ClustalW [46, 47] and Muscle [48] algorithms. These alignments showed highly conserved residues in the sequences of active centre I (CX2CX15CC) and centre II (HX5H-CX2H ). These conversations were translated into “”regular expressions”" that were used to perform for final screening of databases.

Six Syrian hamsters, including three from group A and B (12 wk, 1

Six Syrian hamsters, including three from group A and B (12 wk, 18 wk, and 18 wk, respectively) and three from group C (blank control group), were used as a training group for miRNA microarray analysis. All of the handling measures used with the Syrian hamsters were in accordance with approved guidelines (Guidelines for the Care and Use of Laboratory Animals) established by the Chinese Council on Animal Care. Fabrication of the miRNA microarray The miRNA microarrays were obtained from CapitalBio Corporation (Beijing, China), corresponding to the current release of the Sanger miRNA database (http://​microrna.​sanger.​ac.​uk; August 2007). The individual oligonucleotide probe was learn more printed in triplicate on

chemically modified glass slides in a 21 × 21 spot configuration of MGCD0103 mouse each subarray. The spot diameter was 130 mm, and distance from center to center was 185 mm. A total of 924 mature miRNA sequences were assembled and integrated into our miRNA microarray design. These microarray probes included 677 human miRNAs (including 122 predicted miRNA sequences) [22], 292 rat, and 461 mouse mature miRNAs from the miRNA Registry. All of the oligonucleotide probes

were presented in triplicate in one microarray, and each of the four subarrays contained 16 controls (Zip5, Zip13, Zip15, Zip21, Zip23, Zip25, Y2, Y3, U6, New-U2-R, tRNA-R, hsa-let-7a, hsa-let-7b, hsa-let-7c, 50%DMSO (Dimethyl Sulfoxide), and Hex). The limited sequence length of miRNAs left little consideration for probe design strategy, so all

miRNA probe sequences were designed to be complementary to the full-length mature miRNA. Nucleic acid extraction, labeling, and hybridization Total RNA from each tissue sample was extracted with Trizol reagent (Invitrogen, Carlsbad, USA), and the low-molecular-weight RNA was isolated by a PEG solution precipitation method, according to a previous protocol [23]. We adopted the T4 RNA ligase labeling method according to Thomson’ protocol; that is, 4 μg of low-molecular-weight RNA was labeled with 500 ng of 5′-phosphate-cytidyl-uridyl-cy3-3′ (Dharmacon, Chicago, USA) with 2 units of T4 RNA ligase (NEB, Beijing, China) [24]. The hybridization chamber was laid on a three-phase tiling agitator BioMixerTM II (CapitalBio, Metalloexopeptidase Beijing, China) to promote microfluidic circulation under the coverslip. The hybridization was performed in a water bath at 42°C overnight. The array was then washed with two consecutive washing solutions (0.2% SDS, 2 × SSC at 42°C for 5 min, and 0.2% SSC for 5 min at room temperature). This procedure was repeated twice for each sample. Microarray imaging and data analysis The miRNA microarray from CapitalBio Corporation was a single-channel fluorescence chip; all oligonucleotide probes were labeled with Cy3 fluorescent dye (green). Fluorescence scanning used a double-channel laser scanner (LuxScan 10 K/A, CapitalBio).

A strong correlation (r = 0 94) was found between relative expres

A strong correlation (r = 0.94) was found between relative expression levels obtained by microarray or qRT-PCR SRT1720 cell line analysis (Figure 1). In addition, qRT-PCR experiments performed with RNA extracted from H99 cells FLC-treated at 37°C demonstrated that

expression of the target genes also including AFR1 was comparable to that obtained when H99 cells were pre-treated with FLC at 30°C (Figure 2). Figure 1 Scatter plot of the results by microarray and quantitative RT-PCR analyses for ten selected differentially regulated genes in H99 cells FLC-treated (H99F) compared to untreated control cells. Figure 2 Results of qRT-PCR analysis performed with RNAs extracted from H99 cells FLC-treated (H99F) at 30°C and 37°C. The values, which are means of three separated experiments, represent the increase in gene expression relative to untreated control cells (set YM155 manufacturer at 1.00). Error bars show standard deviations The genes listed in Table 1 were categorized in 10 main groups by functional profiles as described in Methods.

The category with the largest number of genes was “”transport”" with 31 genes, followed by categories that include genes (n = 18) involved in carbohydrate metabolism or protein processes (i.e. biosynthesis, modification, transport and Selleck Volasertib degradation). While up- or down-regulated genes were distributed homogenously within almost all the function groups, some categories included more up-regulated genes

(ergosterol biosynthesis) or down-regulated genes (TCA cycle). As it will be discussed below, the finding of a large number of genes differentially regulated adds support to the concept that azole activity is beyond the inhibition of the lanosterol demethylase target encoded by ERG11 [32], whose overexpression has been associated with fungal resistance [33]. To further classify the genes regulated by FLC exposure, we performed GO term analysis. As expected, GO analysis of genes induced by FLC revealed a significant Edoxaban enrichment of genes involved in sterol metabolism, particularly ergosterol biosynthetic process (Table 2). Enrichment of genes repressed by FLC was observed in processes involving metabolism of amino acids and derivatives (Table 2). Table 2 Gene Ontology (GO) term analysis for the C. neoformans FLC response GO group GO subgroup P-value Up-regulated genes     Oxidation reduction   5.26e-10 Small molecule metabolic process 1.34e-06   Alcohol metabolic process 4.74e-07   Sterol metabolic process 4.41e-07 Steroid metabolic process   7.81e-07   Phytosteroid metabolic process 1.47e-09   Steroid biosynthetic process 9.08e-07   Ergosterol biosynthetic process 3.57e-08 Transmembrane transport   0.00076 Down-regulated genes     Oxidation reduction   1.31e-12 Small molecule metabolic process 2.50e-11   Alcohol metabolic process 0.00037   Cellular ketone metabolic process 1.

3, indicative of negative or purifying selection operating on the

3, indicative of negative or purifying selection operating on these orthologs. A one-way ANOVA demonstrated that the distributions of ω among the four R. sphaeroides strains were

not significantly different from one another (p = 0.920). For the four strains, the mean ω value varied between 0.131 and 0.137 and the standard deviation of ω varied DAPT between 0.030 and 0.037 (pooled S.D. = 0.033). Figure 10 K a -K s correlation of 28 common gene pairs in four R. sphaeroides strains (2.4.1, ATCC 17025, ATCC 17029, and KD131). Ka and Ks values were estimated using MYN (Modified Yang-Nielsen algorithm). ω = 0.3, 1, and 3 were used for negative, neutral, and positive selection, respectively. Horizontal Gene Transfer For R. sphaeroides 2.4.1, the putative HGT regions were found both in CI and CII. The non-optimized 3-deazaneplanocin A purchase coordinates for these regions are not shown. The CI HGT regions sum to 65,005 nucleotides, which spans over 60 genes and which comprises 2.04% of the total CI replicon. The CII HGT regions sum to 110,009 nucleotides,

containing 99 genes, and comprises 11.66% of the total CII replicon. Of the 60 HT genes in CI, 5 are among the duplicate gene pairs, while of the 99 HT genes in CII, 8 are among the duplicate gene pairs. The distribution of HGT regions on both chromosomes revealed that most of the duplicated genes are outside of these HGT regions. Discussion Extent of gene duplication and horizontal gene transfer in R.

sphaeroides A systematic genome analysis of the R. sphaeroides, which possess multiple chromosomes, has shown approximately the same level of gene duplication (~28%) as reported in many other bacterial genomes that possess only one chromosome [22, 42–44] and eukaryotes [22, 45–47]. Thus, similar levels of gene Chorioepithelioma duplication in the genomes of eubacteria, archeae, and eukarya suggest that genome size or genome complexity and the levels of gene duplication present in their genomes are not correlated. Gene duplication can occur on two different scales: large-scale duplication (whole-genome duplication, WGD) and smaller-scale duplications, which consists of tandem duplication of short DNA sequence within a gene, duplication of the entire gene or duplication of large genomic segments [48–50]. The majority of gene duplications in R. sphaeroides exist in the form of small DNA segments (one or few genes), but a few duplications span over a large segment of genomic segments. For example, chemotaxis-related genes are located at four major loci, chemotaxis operon I (RSP2432-RSP2444), chemotaxis operon II (RSP1582-RSP1589), chemotaxis operon III (RSP0042-RSP0049), and chemotaxis operon IV is a part of a 56 kb- flagella biosynthesis gene cluster (RSP0032-RSP0088). Three copies are present on CI and one copy is present on CII.

It was a wonderful period for research in photosynthesis, and Gov

It was a wonderful period for research in photosynthesis, and Govindjee had inherited the “mantle of Robert Emerson” in the study of photosynthetic efficiency (right down to maintaining some of Emerson’s original equipment for measuring quantum efficiency). Some of the questions being asked by the larger community at that time may seem curious or even impossible to today’s generation of researchers—such as, are there 1, 2 or 3 photosystems? I benefited greatly BIBW2992 mouse by my interaction with Govindjee, his students, and our multiple other colleagues who worked on questions of photosynthesis from field studies to quantum mechanics. And, this lively environment made it easy to attract coworkers from

around the world to come and collaborate on projects of mutual interest. It was in this intense but delightful environment that my team identified mechanisms for herbicide resistance in the Photosytem II complex, which lead me to learning

tools of biotechnology for genetic manipulation of proteins. But, this led me away from photosynthesis and into engineering of plants to create pharmaceutically active proteins, which I’ve done for the last 25 years. However, this time for celebration of Govindjee’s career and life causes me to recall those wonderful years in Urbana in the 1970s, and work on chloroplasts and solar energy conversion. Happy Birthday, Govindjee! Eva-Mari Aro Professor of Plant Biology University of Turku, Finland Dear Gov—you are unique! There are not many scientists who can compete with you: (i) in being such a big guy in photosynthesis research; (ii) in being so supportive, helpful and friendly with your colleagues irrespective of their reputation in science; (iii) in supporting young generation scientists; (iv) in having a never-ending enthusiasm for science and bringing that attitude to Turku; (v) in making me edit a book (thanks for that), and finally (vi) in being such a good friend to me. [Eva-Mari Aro and Govindjee have published a research paper on mutagenesis of the D–E loop of the D1 protein (Mulo et al. 1997) and a conference Methamphetamine report where they discovered that the thermoluminescence bands due to see more recombination of Q A − with the S-states were at the same temperature as that due to bands corresponding to recombination involving Q B − in certain mutants of Synechocystis sp. PCC 6803, a rather unusual situation (Keränen et al. 1998); see Fig. 5… JJE-R.] James Barber Ernst Chain Professor of Biochemistry Imperial College London Dear Govindjee I first became aware of you when I was a post-doc in Lou Duysens’ laboratory in Leiden in 1967. Since then our paths have crossed many times. On all occasions you were an inspiration. I admired you not only as an outstanding and committed scientist but also for being so positive and enthusiastic.