The primary structure otE. coliRNA porymerase. Nucleotide sequence of the rpoC gene and amino acid sequence of the β′-sabunit
Author(s) -
Yu.A. Ovchinnikov,
G.S. Monastyrskaya,
В. В. Губанов,
S. O. Guryev,
I. S. Salomatina,
T. M. Shuvaeva,
В. М. Липкин,
E. D. Sverdlov
Publication year - 1982
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/10.13.4035
Subject(s) - biology , nucleic acid sequence , protein primary structure , cyanogen bromide , peptide sequence , microbiology and biotechnology , gene , genetics , transfer rna , coding region , stop codon , rna polymerase , rna , biochemistry
The primary structure of the E. coli rpoC gene (5321 base pairs) coding the beta'-subunit of RNA polymerase as well as its adjacent segment have been determined. The structure analysis of the peptides obtained by cleavage of the protein with cyanogen bromide and trypsin has confirmed the amino acid sequence of the beta'-subunit deduced from the nucleotide sequence analysis. The beta'-subunit of E. coli RNA polymerase contains 1407 amino acid residues. Its translation is initiated by codon GUG and terminated by codon TAA. It has been detected that the sequence following the terminating codon is strikingly homologous to known sequences of rho-independent terminators.
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