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GHKL, an emergent ATPase/kinase superfamily.
A novel ATP-binding superfamily that includes diverse protein families such as DNA topoisomerase II, molecular chaperones Hsp90, DNA-mismatch-repair enzymes MutL and histidine kinases is recognition. Expand
Major cold shock protein of Escherichia coli.
When exponentially growing Escherichia coli cell cultures were transferred from 37 degrees C to 10 degrees C or 15 degrees C, the production of a 7.4-kDa cytoplasmic protein (CS7.4) was prominently induced and revealed that the gene encodes a hydrophilic protein of 70 amino acid residues. Expand
Phylogenetic distribution of branched RNA-linked multicopy single-stranded DNA among natural isolates of Escherichia coli
The hypothesis that msDNA-synthesizing systems, including reverse transcriptase genes, were acquired recently and independently in different lineages of E. coli is supported. Expand
CspA, the Major Cold-shock Protein of Escherichia coli, Is an RNA Chaperone*
It is proposed that CspA functions as an RNA chaperone to prevent the formation of secondary structures in RNA molecules at low temperature and may be crucial for efficient translation of mRNAs at low temperatures and may also have an effect on transcription. Expand
MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli.
It is demonstrated that MazF toxin encoded by "mazEF addiction module" is a sequence-specific (ACA) endoribonuclease functional only for single-stranded RNA, and is, therefore, functionally distinct from RelE, another E. coli toxin, which assists mRNA cleavage at the A site on ribosomes. Expand
Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli.
The requirement for CsdA in derepression of heat-shock protein synthesis is a cold shock-induced function possibly mediated by destabilization of secondary structures previously identified in the rpoH mRNA. Expand
Histidine kinases: diversity of domain organization
The previously known so‐called transmitter domain of histidine kinase is further dissected into two domains: a CA (Catalytic ATP‐binding) domain and a DHp (Dimerization Histidine phosphotransfer) domain for class I, or a CA domain and an HPt (Histidine‐containing PhosphotransFER) domain with significant differences between them. Expand
Acquirement of cold sensitivity by quadruple deletion of the cspA family and its suppression by PNPase S1 domain in Escherichia coli
The present results show that cold‐shock proteins and S1 domains share not only the tertiary structural similarity but also common functional properties, suggesting that these seemingly distinct protein categories may have evolved from a common primordial RNA‐binding protein. Expand
Toxin-antitoxin systems in bacteria and archaea.
Almost all bacteria and many archaea contain genes whose expression inhibits cell growth and may lead to cell death when overproduced, reminiscent of apoptotic genes in higher systems. The cellularExpand
Regulation of growth and death in Escherichia coli by toxin–antitoxin systems
Escherichia coli K-12 contains at least 36 toxin genes, the expression of which causes growth inhibition and eventual death. These toxins are usually co-expressed with their cognate antitoxins inExpand