Cytoplasmic axial filaments in Escherichia coli cells: possible function in the mechanism of chromosome segregation and cell division

Okada, Yoshio; Wachi, Masaaki; Hirata, Akira; Suzuki, Ken‐ichiro; Nagai, Kazuo; Matsuhashi, Michio

doi:10.1128/jb.176.3.917-922.1994

Cited by 62 publications

(53 citation statements)

References 21 publications

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“…In bacteria, in which cytoskeletons have long been undetected, some candidate proteins are appearing recently (1,8). Extracellular organelles such as fragella and pili may be ruled out as candidates for the sonic generator of the cell, since organisms that do not have them such as MM luteus, S cerevisiae and plant cells can also emit (6) and high temperatures.…”

Section: Discussionmentioning

confidence: 99%

Bacillus carboniphilus cells respond to growth-promoting physical signals from cells of homologous and heterologous bacteria.

Matsuhashi

Pankrushina

Endoh³

et al. 1996

J. Gen. Appl. Microbiol.

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Section: Discussionmentioning

confidence: 99%

Bacillus carboniphilus cells respond to growth-promoting physical signals from cells of homologous and heterologous bacteria.

Matsuhashi

Pankrushina

Endoh³

et al. 1996

J. Gen. Appl. Microbiol.

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“…Sounds might be produced by repeated expansion and contraction. This might be accomplished by using intracellular structures, such as membranes, cytoskeleton-like structures (e.g., Casarégola et al, 1990;Okada et al, 1994) or chromosomes, through mechanisms that involve the conversion of ATP or membrane potentials to movement. Activation of an ion channel might be the mechanism for the perception of sound.…”

Section: Discussionmentioning

confidence: 99%

Production of sound waves by bacterial cells and the response of bacterial cells to sound.

Matsuhashi

Pankrushina

Takeuchi

et al. 1998

J. Gen. Appl. Microbiol.

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“…The catalytically active amino-terminal half of the protein (N-RNase E: residues 1-498) is alone sufficient for the enzyme's ribonuclease activity, whereas the carboxyl half of the protein (residues 499-1061) contains both an arginine-rich region and a carboxy-terminal domain that serves as a scaffold for the assembly of a multiprotein complex known as the RNA degradosome (4,5). By contrast, RNase G, which comprises 489 amino acid residues, is similar in sequence to the amino half of RNase E but lacks an arginine-rich region and a scaffold domain (6,7).…”

mentioning

confidence: 99%

Catalytic activation of multimeric RNase E and RNase G by 5′-monophosphorylated RNA

Jiang

Belasco

2004

Proc. Natl. Acad. Sci. U.S.A.

112

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RNase E is an endonuclease that plays a central role in RNA processing and degradation in Escherichia coli. Like its E. coli homolog RNase G, RNase E shows a marked preference for cleaving RNAs that bear a monophosphate, rather than a triphosphate or hydroxyl, at the 5 end. To investigate the mechanism by which 5 -terminal phosphorylation can influence distant cleavage events, we have developed fluorogenic RNA substrates that allow the activity of RNase E and RNase G to be quantified much more accurately and easily than before. Kinetic analysis of the cleavage of these substrates by RNase E and RNase G has revealed that 5 monophosphorylation accelerates the reaction not by improving substrate binding, but rather by enhancing the catalytic potency of these ribonucleases. Furthermore, the presence of a 5 monophosphate can increase the specificity of cleavage site selection within an RNA. Although monomeric forms of RNase E and RNase G can cut RNA, the ability of these enzymes to discriminate between RNA substrates on the basis of their 5 phosphorylation state requires the formation of protein multimers. Among the molecular mechanisms that could account for these properties are those in which 5 -end binding by one enzyme subunit induces a protein structural change that accelerates RNA cleavage by another subunit.M essenger RNAs are labile molecules whose longevity directly influences the synthesis rates of the proteins they encode. Despite the importance of mRNA degradation for gene expression, little is understood about the molecular mechanisms that govern differences in mRNA stability, even in so well studied an organism as Escherichia coli. Elucidating these mechanisms is crucial for explaining how RNA sequence and structure control mRNA lifetimes.The degradation of most E. coli mRNAs is thought to begin with internal cleavage by the endonuclease RNase E (1), although in some cases decay begins instead with cleavage by RNase III or RNase G (an RNase E homolog) (2, 3). The resulting mRNA fragments are then degraded to mononucleotides by a combination of further endonucleolytic cleavage and 3Ј exonucleolytic digestion.RNase E is a 1,061-aa protein comprising functionally distinct domains. The catalytically active amino-terminal half of the protein (N-RNase E: residues 1-498) is alone sufficient for the enzyme's ribonuclease activity, whereas the carboxyl half of the protein (residues 499-1061) contains both an arginine-rich region and a carboxy-terminal domain that serves as a scaffold for the assembly of a multiprotein complex known as the RNA degradosome (4, 5). By contrast, RNase G, which comprises 489 amino acid residues, is similar in sequence to the amino half of RNase E but lacks an arginine-rich region and a scaffold domain (6, 7).In view of the homology of RNase G to the catalytic domain of RNase E, it is not surprising that they have a similar cleavage site specificity, with both preferring to cut RNA within singlestranded regions that are AU-rich (8, 9). Another important property shared by these two en...

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Cytoplasmic axial filaments in Escherichia coli cells: possible function in the mechanism of chromosome segregation and cell division

Cited by 62 publications

References 21 publications

Bacillus carboniphilus cells respond to growth-promoting physical signals from cells of homologous and heterologous bacteria.

Bacillus carboniphilus cells respond to growth-promoting physical signals from cells of homologous and heterologous bacteria.

Production of sound waves by bacterial cells and the response of bacterial cells to sound.

Catalytic activation of multimeric RNase E and RNase G by 5′-monophosphorylated RNA

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