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Cysteinyl-tRNA synthetase: determination of the last E. coli aminoacyl-tRNA synthetase primary structure.

作者信息

Eriani G, Dirheimer G, Gangloff J

机构信息

Institut de Biologie Moléculaire et Cellulaire du CNRS, Strasbourg, France.

出版信息

Nucleic Acids Res. 1991 Jan 25;19(2):265-9. doi: 10.1093/nar/19.2.265.

DOI:10.1093/nar/19.2.265
PMID:2014166
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC333589/
Abstract

The gene coding for E. coli cysteinyl-tRNA synthetase (cysS) was isolated by complementation of a strain deficient in cysteinyl-tRNA synthetase activity at high temperature (43 degrees C). Sequencing of a 2.1 kbp DNA fragment revealed an open reading frame of 1383 bp coding for a protein of 461 amino acid residues with a Mr of 52,280, a value in close agreement with that observed for the purified protein, which behaves as a monomer. The sequence of CysRS bears the canonical His-Ile- Gly -His (HIGH) and Lys-Met-Ser-Lys-Ser (KMSKS) motifs characteristic of the group of enzymes containing a Rossmann fold; furthermore, it shows striking homologies with MetRS (an homodimer of 677 residues) and to a lesser extent with Ile-, Leu-, and ValRS (monomers of 939, 860, and 951 residues respectively). With its monomeric state and smaller size, CysRS is probably more closely related to the primordial aminoacyl-tRNA synthetase from which all have diverged.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f6bf/333589/f66dda5f4f78/nar00238-0067-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f6bf/333589/f66dda5f4f78/nar00238-0067-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f6bf/333589/f66dda5f4f78/nar00238-0067-a.jpg

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本文引用的文献

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