Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in <i>Escherichia coli</i>

Morita, Teppei; Kawamoto, Hiroshi; Mizota, Taisei; Inada, Toshifumi; Aiba, Hirofumi

doi:10.1111/j.1365-2958.2004.04329.x

Cited by 156 publications

(162 citation statements)

References 45 publications

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“…shown to perform a crucial function in the regulation of RNA degradation (12). It also involved tRNA transport to the mitochondria in yeast (13).…”

Section: Features Of Heat-stable Proteins In E Colimentioning

confidence: 99%

Proteomic analysis of heat-stable proteins in Escherichia coli

Kwon¹,

Jung²,

Lim³

2008

BMB Reports

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Some proteins of E. coli are stable at temperatures significantly higher than 49 o C, the maximum temperature at which the organism can grow. The heat stability of such proteins would be a property which is inherent to their structures, or it might be acquired by evolution for their specialized functions. In this study, we describe the identification of 17 heat-stable proteins from E. coli. Approximately one-third of these proteins were recognized as having functions in the protection of other proteins against denaturation. These included chaperonin (GroEL and GroES), molecular chaperones (DnaK and FkpA) and peptidyl prolyl isomerases (trigger factor and FkpA). Another common feature was that five of these proteins (GroEL, GroES, Ahpc, RibH and ferritin) have been shown to form a macromolecular structure. These results indicated that the heat stability of certain proteins may have evolved for their specialized functions, allowing them to cope with harsh environments, including high temperatures. [BMB reports 2008; 41(2): 108-111]

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“…shown to perform a crucial function in the regulation of RNA degradation (12). It also involved tRNA transport to the mitochondria in yeast (13).…”

Section: Features Of Heat-stable Proteins In E Colimentioning

confidence: 99%

Proteomic analysis of heat-stable proteins in Escherichia coli

Kwon¹,

Jung²,

Lim³

2008

BMB Reports

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“…PtsG mRNA degradation is dependent upon RNase E and Hfq in an RNase E-Hfq-SgrS ribonucleoprotein complex (Morita et al 2003(Morita et al , 2004(Morita et al , 2006. As a consequence, an hfq mutant is unable to initiate the phosphostress response and does not grow on plates containing αMG (Fig.…”

Section: Cd-hfq Does Not Trigger Ptsg Control By Sgrsmentioning

confidence: 99%

Clostridium difficile Hfq can replace Escherichia coli Hfq for most of its function

Caillet

Gracia

Fontaine

et al. 2014

RNA

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A gene for the Hfq protein is present in the majority of sequenced bacterial genomes. Its characteristic hexameric ring-like core structure is formed by the highly conserved N-terminal regions. In contrast, the C-terminal forms an extension, which varies in length, lacks homology, and is predicted to be unstructured. In Gram-negative bacteria, Hfq facilitates the pairing of sRNAs with their mRNA target and thus affects gene expression, either positively or negatively, and modulates sRNA degradation. In Gram-positive bacteria, its role is still poorly characterized. Numerous sRNAs have been detected in many Gram-positive bacteria, but it is not yet known whether these sRNAs act in association with Hfq. Compared with all other Hfqs, the C. difficile Hfq exhibits an unusual C-terminal sequence with 75% asparagine and glutamine residues, while the N-terminal core part is more conserved. To gain insight into the functionality of the C. difficile Hfq (Cd-Hfq) protein in processes regulated by sRNAs, we have tested the ability of Cd-Hfq to fulfill the functions of the E. coli Hfq (Ec-Hfq) by examining various functions associated with Hfq in both positive and negative controls of gene expression. We found that Cd-Hfq substitutes for most but not all of the tested functions of the Ec-Hfq protein. We also investigated the role of the C-terminal part of the Hfq proteins. We found that the C-terminal part of both Ec-Hfq and Cd-Hfq is not essential but contributes to some functions of both the E. coli and C. difficile chaperons.

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“…Finally, in E.coli, enolase is an integral component of the RNA degradosome (Kuhnel and Luisi 2001;Carpousis 2002). Its role was hypothesized to direct subcellular compartmentalization of degradosome to the plasma membrane (Liou et al 2001;Morita et al 2004).…”

Section: Enolase Another Protein With Multiple Functionsmentioning

confidence: 99%

A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae

Entelis¹,

Brandina²,

Kamenski³

et al. 2006

Genes Dev.

156

134

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In many organisms, mitochondria import nuclear DNA-encoded small RNAs. In yeast Saccharomyces cerevisiae, one out of two cytoplasmic isoacceptor tRNAs Lys is partially addressed into the organelle. Mitochondrial targeting of this tRNA was shown to depend on interaction with the precursor of mitochondrial lysyl-tRNA synthetase, preMsk1p. However, preMsk1p alone was unable to direct tRNA targeting, suggesting the existence of additional protein factor(s). Here, we identify the glycolytic enzyme, enolase, as such a factor. We demonstrate that recombinant enolase and preMSK1p are sufficient to direct tRNA import in vitro and that depletion of enolase inhibits tRNA import in vivo. Enzymatic and tRNA targeting functions of enolase appear to be independent. Three newly characterized properties of the enolase can be related to its novel function: (1) specific affinity to the imported tRNA, (2) the ability to facilitate formation of the complex between preMsk1p and the imported tRNA, and (3) partial targeting toward the mitochondrial outer membrane. We propose a model suggesting that the cell exploits mitochondrial targeting of the enolase in order to address the tRNA toward peri-mitochondrially synthesized preMsk1p. Our results indicate an alternative molecular chaperone function of glycolytic enzyme enolase in tRNA mitochondrial targeting.

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Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli

Cited by 156 publications

References 45 publications

Proteomic analysis of heat-stable proteins in Escherichia coli

Proteomic analysis of heat-stable proteins in Escherichia coli

Clostridium difficile Hfq can replace Escherichia coli Hfq for most of its function

A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae

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