The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

proS  -  prolyl-tRNA synthetase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0194, JW0190, drpA
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of proS


High impact information on proS

  • The existence of this protein contrasts with proposals that aminoacylation with cysteine in M. jannaschii is an auxiliary function of a canonical prolyl-tRNA synthetase [2].
  • The R197 M mutant enzyme catalyzed removal of the proS hydrogen atom from (4'R)-[(3)H]PMP, showing that the guanidinium side-chain plays an important role in determining stereospecificity [3].
  • To identify potential acceptor stem contacts made by Escherichia coli prolyl-tRNA synthetase (ProRS), an enzyme of unknown structure, we performed cysteine-scanning mutagenesis in the motif 2 loop [4].
  • Our data suggest that the two ProRS groups may reflect coadaptations needed to accommodate changes in the operational RNA code for proline [5].
  • We establish that the drpA gene has been successfully cloned and describe the fine-structure map of three drpA-(Ts) mutations as well as the complete nucleotide sequence of the drpA gene [6].

Biological context of proS

  • We identified a major sigma-70 promoter for the drpA gene on the bases of (i) its similarity to the consensus sequence and (ii) S1 protection and primer extension mapping data [6].
  • The plasmid has been used to clone part of a homologue of the E. coli drpA gene, encoding a global regulatory element for RNA synthesis [7].
  • Alignment of all known ProRS primary sequences from different species reveals particularly low overall sequence homology, as well as two distinct groups of enzymes [8].

Anatomical context of proS

  • The possibility that the largest subunit of the mammalian high-M(r) complexes may be a bifunctional protein encoding both glutamyl- and prolyl-tRNA synthetase activities is considered and discussed in light of the recently published sequence of the corresponding polypeptide from HeLa cells [9].


  1. A dual-specificity aminoacyl-tRNA synthetase in the deep-rooted eukaryote Giardia lamblia. Bunjun, S., Stathopoulos, C., Graham, D., Min, B., Kitabatake, M., Wang, A.L., Wang, C.C., Vivarès, C.P., Weiss, L.M., Söll, D. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  2. An aminoacyl tRNA synthetase whose sequence fits into neither of the two known classes. Fàbrega, C., Farrow, M.A., Mukhopadhyay, B., de Crécy-Lagard, V., Ortiz, A.R., Schimmel, P. Nature (2001) [Pubmed]
  3. Active site structure and stereospecificity of Escherichia coli pyridoxine-5'-phosphate oxidase. di Salvo, M.L., Ko, T.P., Musayev, F.N., Raboni, S., Schirch, V., Safo, M.K. J. Mol. Biol. (2002) [Pubmed]
  4. Evolutionary coadaptation of the motif 2--acceptor stem interaction in the class II prolyl-tRNA synthetase system. Burke, B., Yang, F., Chen, F., Stehlin, C., Chan, B., Musier-Forsyth, K. Biochemistry (2000) [Pubmed]
  5. Species-specific differences in the operational RNA code for aminoacylation of tRNAPro. Stehlin, C., Burke, B., Yang, F., Liu, H., Shiba, K., Musier-Forsyth, K. Biochemistry (1998) [Pubmed]
  6. Identification and sequence of the drpA gene from Escherichia coli. Zhou, Z., Syvanen, M. J. Bacteriol. (1990) [Pubmed]
  7. A medium-copy-number plasmid for insertional mutagenesis of Streptococcus mutans. Sanchez, R. Plasmid (1998) [Pubmed]
  8. Understanding species-specific differences in substrate recognition by Escherichia coli and human prolyl-tRNA synthetases. Musier-Forsyth, K., Stehlin, C., Burke, B., Liu, H. Nucleic Acids Symp. Ser. (1997) [Pubmed]
  9. Mammalian prolyl-tRNA synthetase corresponds to the approximately 150 kDa subunit of the high-M(r) aminoacyl-tRNA synthetase complex. Kerjan, P., Triconnet, M., Waller, J.P. Biochimie (1992) [Pubmed]
WikiGenes - Universities