Structure of GlgS from Escherichia coli suggests a role in protein–protein interactions

Kozlov, Guennadi; Elias, Demetra; Cygler, Mirosław; Gehring, Kalle

doi:10.1186/1741-7007-2-10

BMC Biol

2004

DOI: 10.1186/1741-7007-2-10

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Structure of GlgS from Escherichia coli suggests a role in protein–protein interactions

Guennadi Kozlov

Demetra Elias

Mirosław Cygler

et al.

Abstract: Background: The Escherichia coli protein GlgS is up-regulated in response to starvation stress and its overexpression was shown to stimulate glycogen synthesis.

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Cited by 9 publications

(1 citation statement)

References 29 publications

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“…Interestingly, a structural homology search using the DALI database [28] did not identify any known protein of comparable length displaying the two-helix fold predicted for DDEE-C 1 A 2 B 2 . However, some structural homology is detected between DDEE-A 2 B 2 C 1 and a subdomain of the E. coli protein GlgS [29]. The latter is a 66-residues protein possessing a three-helix bundle fold with a long-bent helix.…”

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confidence: 95%

The Production ofde novo Folded Proteins by a Stepwise Chain Elongation: A Model for Prebiotic Chemical Evolution of Macromolecular Sequences

Chessari

Thomas

Polticelli

et al. 2006

C&B

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We describe an experimental procedure to mimic the formation of long (over 40 residues) co-oligopetide sequences in many identical copies which may have occurred in the prebiotic molecular evolution. The basic hypothesis is that chain formation is based on the stepwise fragment condensation of randomly generated short oligopeptides, whereby the elongation takes place under the contingent environmental constraints (solubility, pH, salinity), which eliminate most of the products, and thus determine the selection towards one particular small set of chains. The present work aims at verifying the validity of this scheme. In order to do so, we utilize a classic synthetic procedure based on the Merrifield solid-phase synthesis of peptides for the synthesis of randomly produced peptides as well as for their stepwise fragment condensation. Thus, starting from a library of peptides with n=10, the first condensation step produces a library of 16 peptides with 20 residues each (n=20), of which only four remain water-soluble and, therefore, capable to undergo the next fragment condensation step. This gives rise to 16 peptides with n=30, out of which twelve precipitate out under the chosen pH and buffer conditions and are eliminated. Finally, a 44-residue-long water-soluble de novo protein is obtained. This has no homologies or similarities with extant proteins, and, based on circular dichroism (CD), it assumes a stable three-dimensional folding. In agreement with CD data, molecular-modelling simulations suggest an helical fold for the protein with poor, if any, structural homology with known proteins. The implication of this procedure as a general mechanism for the etiology of de novo macromolecular sequences and globular proteins in the origin of life is briefly discussed.

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mentioning

confidence: 95%

The Production ofde novo Folded Proteins by a Stepwise Chain Elongation: A Model for Prebiotic Chemical Evolution of Macromolecular Sequences

Chessari

Thomas

Polticelli

et al. 2006

C&B

View full text Add to dashboard Cite

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Post-transcriptional global regulation by CsrA in bacteria

Timmermans

Melderen

2010

Cell. Mol. Life Sci.

156

177

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Global regulation allows bacteria to rapidly modulate the expression of a large variety of unrelated genes in response to environmental changes. Global regulators act at different levels of gene expression. This review focuses on CsrA, a post-transcriptional regulator that affects translation of its gene targets by binding mRNAs. CsrA controls a large variety of physiological processes such as central carbon metabolism, motility and biofilm formation. The activity of CsrA is itself tightly regulated by the CsrB and CsrC small RNAs and the BarA-UvrY two-component system.

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Glycogen with short average chain length enhances bacterial durability

Wang

Wise

2011

Naturwissenschaften

136

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Glycogen is conventionally viewed as an energy reserve that can be rapidly mobilized for ATP production in higher organisms. However, several studies have noted that glycogen with short average chain length in some bacteria is degraded very slowly. In addition, slow utilization of glycogen is correlated with bacterial viability, that is, the slower the glycogen breakdown rate, the longer the bacterial survival time in the external environment under starvation conditions. We call that a durable energy storage mechanism (DESM). In this review, evidence from microbiology, biochemistry, and molecular biology will be assembled to support the hypothesis of glycogen as a durable energy storage compound. One method for testing the DESM hypothesis is proposed.

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Structure of GlgS from Escherichia coli suggests a role in protein–protein interactions

Abstract: Background: The Escherichia coli protein GlgS is up-regulated in response to starvation stress and its overexpression was shown to stimulate glycogen synthesis.

Cited by 9 publications

References 29 publications

The Production ofde novo Folded Proteins by a Stepwise Chain Elongation: A Model for Prebiotic Chemical Evolution of Macromolecular Sequences

The Production ofde novo Folded Proteins by a Stepwise Chain Elongation: A Model for Prebiotic Chemical Evolution of Macromolecular Sequences

Post-transcriptional global regulation by CsrA in bacteria

Glycogen with short average chain length enhances bacterial durability

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