YmdB: a stress-responsive ribonuclease-binding regulator of E. coli RNase III activity
YmdB: a stress-responsive ribonuclease-binding regulator of E. coli RNase III activity
复制标题
DOI:
10.1101/gad.1729508
复制
发表时间:
2008-12-15
影响因子:
10.5
通讯作者:
Cohen, Stanley N.
中科院分区:
文献类型:
--
作者:
Kim, Kwang-Sun;Manasherob, Robert;Cohen, Stanley N.
The broad cellular actions of RNase III family enzymes include ribosomal RNA ( rRNA) processing, mRNA decay, and the generation of noncoding microRNAs in both prokaryotes and eukaryotes. Here we report that YmdB, an evolutionarily conserved 18.8-kDa protein of Escherichia coli of previously unknown function, is a regulator of RNase III cleavages. We show that YmdB functions by interacting with a site in the RNase III catalytic region, that expression of YmdB is transcriptionally activated by both cold-shock stress and the entry of cells into stationary phase, and that this activation requires the sigma-factor-encoding gene, rpoS. We discovered that down-regulation of RNase III activity occurs during both stresses and is dependent on YmdB production during cold shock; in contrast, stationary-phase regulation was unperturbed in ymdB-null mutant bacteria, indicating the existence of additional, YmdB-independent, factors that dynamically regulate RNase III actions during normal cell growth. Our results reveal the previously unsuspected role of ribonuclease-binding proteins in the regulation of RNase III activity.