Open AccessNudeotide sequenee of therpoA-rplQDNA ofEscherichia coli: a second regulalory binding site for protein S4?
Author(s) -
David W. Meek,
Richard S. Hayward
Publication year - 1984
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/12.14.5813
Subject(s) - operon , biology , rna polymerase , gene , genetics , ribosomal protein , transcription (linguistics) , escherichia coli , microbiology and biotechnology , ribosomal rna , binding site , dna , messenger rna , rna , ribosome , linguistics , philosophy
The "alpha-operon" of E.coli is a unit of regulation comprising the following known genes, mostly encoding ribosomal proteins (in order of transcription, and with their products named in brackets): rpsM (S13), rpsK (S11), rpsD (S4), rpoA (alpha-subunit of RNA polymerase), rplQ (L17). There is evidence that S4 tightly regulates all of these genes, except rpoA, by repressing translation of the polycistronic mRNA. Binding of S4 to the S13 start-site is thought to regulate the first three genes. We have extended the 'rpsD-rpoA' sequences previously determined by others, to include all of rpoA and rplQ. The rpoA-rplQ intercistronic region shows strong primary, and potential secondary structural homologies with the S4-binding sites on 16S rRNA and S13 mRNA. We suggest that S4 represses L17 translation directly.