Nucleotide sequence of the rplJL operon and the deduced primary structure of the encoded L10 and L7/L12 proteins of Salmonella typhimurium compared to that of Escherichia coli
Author(s) -
A. N. Zhyvoloup,
M. I. Woodmaska,
I. V. Kroupskaya,
Е. Б. Патон
Publication year - 1990
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/18.15.4620
Subject(s) - biology , nucleic acid sequence , operon , protein primary structure , genetics , escherichia coli , sequence (biology) , peptide sequence , salmonella , nucleotide , enterobacteriaceae , base sequence , l arabinose operon , gene , microbiology and biotechnology , bacteria
Portions of the S. typhimurium rpUL operon were isolated by EcoRI digestion from the recombinant pNL1 plasmid (1), cloned on the pUC19 vector (2) and sequenced by the procedure (3). Presented below is the determined nucleotide sequence of rpUL and the deduced a. a. sequence of r-proteins LlO and L7/L12 of S. typhimurium, as compared to those of E. coli (4). Due to the highly conserved structure, LlO protein of S. typhimurium is regulatory capable for rpUL genes of E. coli (5). Only three a.a. (Ser-12, Ala-45 and Ser-109) are different in L7/L12 protein of S. typhimurium and E. coli. In contrast to the leader sequence of the rlpJL mRNA and the LlO-binding site (overlined) (6), no EMBL accession no. X53072
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