Genomes and Genes
Gene Symbol: proS
Description: prolyl-tRNA synthetase
Alias: ECK0194, JW0190, drpA
Species: Escherichia coli str. K-12 substr. MG1655
- Ibba M, Soll D. Aminoacyl-tRNA synthesis. Annu Rev Biochem. 2000;69:617-50 pubmed..This article reviews current knowledge of the biochemical, structural, and evolutionary facets of aminoacyl-tRNA synthesis. ..
- Zheng Y, Roberts R, Kasif S. Segmentally variable genes: a new perspective on adaptation. PLoS Biol. 2004;2:E81 pubmed..Discerning their function and identifying their binding partners may offer biologists new insights into the basic mechanisms of adaptation, context-dependent evolution, and the interaction between microbes and their environment. ..
- Hati S, Ziervogel B, Sternjohn J, Wong F, Nagan M, Rosen A, et al. Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in "selective release" of noncognate amino acids. J Biol Chem. 2006;281:27862-72 pubmed
- Papas T, Mehler A. Kinetic studies of the prolyl transfer ribonucleic acid synthetase of Escherichia coli. Order of addition of substrates and release of products. J Biol Chem. 1971;246:5924-8 pubmed
- Splan K, Ignatov M, Musier Forsyth K. Transfer RNA modulates the editing mechanism used by class II prolyl-tRNA synthetase. J Biol Chem. 2008;283:7128-34 pubmed publisher..Taken together, the results reported herein illustrate how both pre- and post-transfer editing pathways work in concert to ensure accurate aminoacylation by ProRS. ..
- Stehlin C, Heacock D, Liu H, Musier Forsyth K. Chemical modification and site-directed mutagenesis of the single cysteine in motif 3 of class II Escherichia coli prolyl-tRNA synthetase. Biochemistry. 1997;36:2932-8 pubmed
- Eriani G, Delarue M, Poch O, Gangloff J, Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature. 1990;347:203-6 pubmed..Surprisingly, this partition of aaRS in two classes is found to be strongly correlated on the functional level with the acylation occurring either on the 2' OH (class I) or 3' OH (class II) of the ribose of the last nucleotide of tRNA. ..
- Cusack S, Hartlein M, Leberman R. Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. Nucleic Acids Res. 1991;19:3489-98 pubmed
- Depping R, Lohaus C, Meyer H, Rüger W. The mono-ADP-ribosyltransferases Alt and ModB of bacteriophage T4: target proteins identified. Biochem Biophys Res Commun. 2005;335:1217-23 pubmed..E. coli trigger factor and the elongation factor EF-Tu were 2 targets of ModB action, and these proteins were among the 10 identified as targets of Alt, hinting that these factors are involved in phage replication. ..
- Beuning P, Musier Forsyth K. Hydrolytic editing by a class II aminoacyl-tRNA synthetase. Proc Natl Acad Sci U S A. 2000;97:8916-20 pubmed..We show here that C443 is critical for the hydrolytic editing of Ala-tRNA(Pro) by this class II synthetase. ..
- Jacquin Becker C, Ahel I, Ambrogelly A, Ruan B, Soll D, Stathopoulos C. Cysteinyl-tRNA formation and prolyl-tRNA synthetase. FEBS Lett. 2002;514:34-6 pubmed..Here we review our current knowledge of this fascinating process. ..
- Archibold E, Williams L. Regulation of synthesis of methionyl-, prolyl-, and threonyl-transfer ribonucleic acid synthetases of Escherichia coli. J Bacteriol. 1972;109:1020-6 pubmed..These results support previous findings and further strengthen the idea that the formation of aminoacyl-tRNA synthetases is regulated by some mechanism which is mediated by the cognate amino acids. ..
- Lech K, Lee C, Isberg R, Syvanen M. New gene in Escherichia coli K-12 (drpA): does its product play a role in RNA synthesis?. J Bacteriol. 1985;162:117-23 pubmed..Using transposon Tn5 mutagenesis of this plasmid, we have been able to correlate the presence of a 68-kilodalton protein, as observed with the maxicell technique, with the ability of this plasmid to restore growth to drpA1 mutants. ..
- Wolf Y, Aravind L, Grishin N, Koonin E. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res. 1999;9:689-710 pubmed
- Hasegawa T, Yokogawa T. Escherichia coli proline tRNA: structure and recognition sites for prolyl-tRNA synthetase. Nucleic Acids Symp Ser. 2000;:7-8 pubmed
- Bohman K, Isaksson L. A temperature-sensitive mutant in prolinyl-tRNA ligase of Escherichia coli K-12. Mol Gen Genet. 1980;177:603-5 pubmedA mutant with a defective prolinyl-tRNA ligase has been found in a collection of spontaneous temperature-sensitive mutants. The mutated gene, which is designated proS, is closely linked to metD.
- Johnson J, Sanford B, Strom A, Tadayon S, Lehman B, Zirbes A, et al. Multiple pathways promote dynamical coupling between catalytic domains in Escherichia coli prolyl-tRNA synthetase. Biochemistry. 2013;52:4399-412 pubmed publisher..Free energy analysis revealed that communication between residues within a pathway and cross-talk between pathways are important for coordinating functions of different domains of Ec ProRS for efficient catalysis...
- Sternjohn J, Hati S, Siliciano P, Musier Forsyth K. Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain. Proc Natl Acad Sci U S A. 2007;104:2127-32 pubmed..In this manner, a single editing module can be distributed to different synthetases, and simultaneously acquire specificity and enhanced activity. ..
- Papas T, Mehler A. Analysis of the amino acid binding to the proline transfer ribonucleic acid synthetase of Escherichia coli. J Biol Chem. 1970;245:1588-95 pubmed
- Zhou Z, Syvanen M. Identification and sequence of the drpA gene from Escherichia coli. J Bacteriol. 1990;172:281-6 pubmedThe drpA gene of Escherichia coli encodes a factor that is involved in global RNA synthesis...
- Liu H, Yap L, Stehlin C, Musier Forsyth K. Molecular recognition of tRNA(Pro) by Escherichia coli proline-tRNA synthetase. Nucleic Acids Symp Ser. 1995;:176-8 pubmed..We have also identified a specific 2'-hydroxyl-base interaction between the ribose of U8 and the 2-amino group of G46 that makes a thermodynamically significant contribution to tRNA(Pro) aminoacylation by E. coli ProRS. ..
- Lee M, Muench K. Prolyl transfer ribonucleic acid synthetase of Escherichia coli. I. Purification and evidence for subunits. J Biol Chem. 1969;244:223-30 pubmed
- Ruan B, Palioura S, Sabina J, Marvin Guy L, Kochhar S, LaRossa R, et al. Quality control despite mistranslation caused by an ambiguous genetic code. Proc Natl Acad Sci U S A. 2008;105:16502-7 pubmed publisher..In this way, E. coli ensures the presence of sufficient functional protein albeit at a considerable energetic cost. ..