proS

Summary

Gene Symbol: proS
Description: prolyl-tRNA synthetase
Alias: ECK0194, JW0190, drpA
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Liu H, Musier Forsyth K. Escherichia coli proline tRNA synthetase is sensitive to changes in the core region of tRNA(Pro). Biochemistry. 1994;33:12708-14 pubmed
    ..In particular, nucleotides in the D-loop and backbone functional groups in the D-stem appear to be critical for maintaining a tRNA structure that is optimal for recognition by proline tRNA synthetase in vitro. ..
  2. Burke B, Yang F, Chen F, Stehlin C, Chan B, Musier Forsyth K. Evolutionary coadaptation of the motif 2--acceptor stem interaction in the class II prolyl-tRNA synthetase system. Biochemistry. 2000;39:15540-7 pubmed
    ..Taken together, our results illustrate how synthetases and tRNAs have coadapted to changes in protein-acceptor stem recognition through evolution. ..
  3. Wong F, Beuning P, Nagan M, Shiba K, Musier Forsyth K. Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editing. Biochemistry. 2002;41:7108-15 pubmed
    ..Our biochemical data and modeling studies suggest that the prokaryotic INS plays a critical role in editing and that this activity resides in a domain that is functionally and structurally distinct from the aminoacylation active site. ..
  4. Yap L, Stehlin C, Musier Forsyth K. Use of semi-synthetic transfer RNAs to probe molecular recognition by Escherichia coli proline-tRNA synthetase. Chem Biol. 1995;2:661-6 pubmed
    ..coli ProRS. ProRS is also sensitive to changes that are likely to alter the helical conformation in the T psi C stem. ..
  5. Wong F, Beuning P, Silvers C, Musier Forsyth K. An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing. J Biol Chem. 2003;278:52857-64 pubmed
    ..Thus, we demonstrate for the first time that an independently folded class II synthetase editing domain and a previously identified homolog can catalyze a hydrolytic editing reaction. ..
  6. McClain W, Schneider J, Gabriel K. Distinctive acceptor-end structure and other determinants of Escherichia coli tRNAPro identity. Nucleic Acids Res. 1994;22:522-9 pubmed
    ..The results speak for the importance of a distinctive conformation in the acceptor-stem helix of tRNAPro for aminoacylation by the prolyl-tRNA synthetase. The anticodon also contributes to tRNAPro identity but is not necessary in vivo. ..
  7. Liu H, Peterson R, Kessler J, Musier Forsyth K. Molecular recognition of tRNA(Pro) by Escherichia coli proline tRNA synthetase in vitro. Nucleic Acids Res. 1995;23:165-9 pubmed
    ..Moreover, bases that are believed to be important for maintaining the tertiary structure of the tRNA (G15 and C48) appear to be important for efficient recognition of tRNA(Pro) by ProRS in vitro. ..
  8. Yap L, Musier Forsyth K. Transfer RNA aminoacylation: identification of a critical ribose 2'-hydroxyl-base interaction. RNA. 1995;1:418-24 pubmed
    ..This is the first study to identify a specific ribose 2'-hydroxyl-base interaction in the core region of a tRNA molecule that makes a thermodynamically significant contribution to aminoacylation. ..
  9. Ahel I, Stathopoulos C, Ambrogelly A, Sauerwald A, Toogood H, Hartsch T, et al. Cysteine activation is an inherent in vitro property of prolyl-tRNA synthetases. J Biol Chem. 2002;277:34743-8 pubmed publisher
    ..Therefore, ProRS exhibits a natural level of mischarging that is to date unequalled among the aminoacyl-tRNA synthetases...

More Information

Publications34

  1. 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. ..
  2. 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. ..
  3. 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
  4. 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
  5. 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. ..
  6. 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
  7. Burke B, An S, Musier Forsyth K. Functional guanine-arginine interaction between tRNAPro and prolyl-tRNA synthetase that couples binding and catalysis. Biochim Biophys Acta. 2008;1784:1222-5 pubmed publisher
  8. 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. ..
  9. 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
  10. Depping R, Lohaus C, Meyer H, RĂ¼ger 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. ..
  11. 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. ..
  12. 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. ..
  13. 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. ..
  14. 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. ..
  15. 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
  16. Hasegawa T, Yokogawa T. Escherichia coli proline tRNA: structure and recognition sites for prolyl-tRNA synthetase. Nucleic Acids Symp Ser. 2000;:7-8 pubmed
  17. Bohman K, Isaksson L. A temperature-sensitive mutant in prolinyl-tRNA ligase of Escherichia coli K-12. Mol Gen Genet. 1980;177:603-5 pubmed
    A 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.
  18. An S, Barany G, Musier Forsyth K. Evolution of acceptor stem tRNA recognition by class II prolyl-tRNA synthetase. Nucleic Acids Res. 2008;36:2514-21 pubmed publisher
  19. 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...
  20. 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. ..
  21. 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
  22. Zhou Z, Syvanen M. Identification and sequence of the drpA gene from Escherichia coli. J Bacteriol. 1990;172:281-6 pubmed
    The drpA gene of Escherichia coli encodes a factor that is involved in global RNA synthesis...
  23. 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. ..
  24. 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
  25. 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. ..