Characterisation of mutations in GroES that allow GroEL to function as a single ring

Liu, Han; Kovács, Eszter; Lund, Peter A.

doi:10.1016/j.febslet.2009.06.027

Cited by 17 publications

(18 citation statements)

References 35 publications

(57 reference statements)

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“…Based on the genetic and biochemical analyses presented in this study, the single groES gene was indispensable for M. xanthus cells, and the stand-alone groEL gene still required groES in order to function. Generally, each of the GroEL1 and GroEL2 proteins was able to form a 14-mer complex, which further bound to a 7-mer polymer of the GroES protein in vivo , consistent with that in the bacteria possessing single groEL and groES genes (Weissman et al, 1995; Liu et al, 2009). In the absence of GroES, the DK1622 GroEL proteins were unable to refold denatured proteins correctly in vitro and in vivo .…”

Section: Discussionsupporting

confidence: 67%

Myxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroES

Wang

Zheng

et al. 2017

Front. Microbiol.

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Chaperonin GroEL (Cpn60) requires cofactor GroES (Cpn10) for protein refolding in bacteria that possess single groEL and groES genes in a bicistronic groESL operon. Among 4,861 completely-sequenced prokaryotic genomes, 884 possess duplicate groEL genes and 770 possess groEL genes with no neighboring groES. It is unclear whether stand-alone groEL requires groES in order to function and, if required, how duplicate groEL genes and unequal groES genes balance their expressions. In Myxococcus xanthus DK1622, we determined that, while duplicate groELs were alternatively deletable, the single groES that clusters with groEL1 was essential for cell survival. Either GroEL1 or GroEL2 required interactions with GroES for in vitro and in vivo functions. Deletion of groEL1 or groEL2 resulted in decreased expressions of both groEL and groES; and ectopic complementation of groEL recovered not only the groEL but also groES expressions. The addition of an extra groES gene upstream groEL2 to form a bicistronic operon had almost no influence on groES expression and the cell survival rate, whereas over-expression of groES using a self-replicating plasmid simultaneously increased the groEL expressions. The results indicated that M. xanthus DK1622 cells coordinate expressions of the duplicate groEL and single groES genes for synergistic functions of GroELs and GroES. We proposed a potential regulation mechanism for the expression coordination.

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Section: Discussionsupporting

confidence: 67%

Myxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroES

Wang

Zheng

et al. 2017

Front. Microbiol.

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“…S3B). Our observations that substitutions at Ile-25 in GroES 7 are more effective than those at Val-26 or Leu-27 in activating MDH folding activity of GroEL SR parallel results from genetic studies (36 …”

Section: Groelsupporting

confidence: 76%

“…The folding active GroEL SR -GroES systems consist of variants of GroEL SR , identified from genetic analysis (34 -37), or variants of GroES, identified from random mutagenesis study on the GroEL-binding GroES mobile loop (36). Reduced GroEL-GroES interaction has been implicated in these folding active GroEL SR -GroES variants; however, the basis for the mutational effect is not immediately clear.…”

mentioning

confidence: 99%

Stimulating the Substrate Folding Activity of a Single Ring GroEL Variant by Modulating the Cochaperonin GroES

Illingworth

Ramsey

Zheng

2011

Journal of Biological Chemistry

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In mediating protein folding, chaperonin GroEL and cochaperonin GroES form an enclosed chamber for substrate proteins in an ATP-dependent manner. The essential role of the double ring assembly of GroEL is demonstrated by the functional deficiency of the single ring GroEL SR . The GroEL SR -GroES is highly stable with minimal ATPase activity. To restore the ATP cycle and the turnover of the folding chamber, we sought to weaken the GroEL SR -GroES interaction systematically by concatenating seven copies of groES to generate groES 7 . GroES Ile-25, Val-26, and Leu-27, residues on the GroEL-GroES interface, were substituted with Asp on different groES modules of groES 7 . GroES 7

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“…In addition, Glu461, involved in the coevolution between Ala260 and Arg268, has a role in stabilizing inter-ring contacts [41]. Since GroES is heavily involved in determining the function of GroEL as a single or as a double ring [33], the coevolution of Glu461 from GroEL with GroES amino acid sites may have implications in the structural stability of the double ring, and thus, GroES-GroEL folding cycle.…”

Section: Resultsmentioning

confidence: 99%

“…The gene groEL has undergone many duplications in bacteria [2], adaptive evolution [31] and functional divergence [32]. Moreover, structural evolutionary changes have been recently described for GroEL, according to which changes in the amino acid composition of its co-chaperonin GroES can determine GroEL functioning as a single instead of double ring [33]. …”

Section: Introductionmentioning

confidence: 99%

Coevolution analyses illuminate the dependencies between amino acid sites in the chaperonin system GroES-L

Ruiz-González

Fares

2013

BMC Evol Biol

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BackgroundGroESL is a heat-shock protein ubiquitous in bacteria and eukaryotic organelles. This evolutionarily conserved protein is involved in the folding of a wide variety of other proteins in the cytosol, being essential to the cell. The folding activity proceeds through strong conformational changes mediated by the co-chaperonin GroES and ATP. Functions alternative to folding have been previously described for GroEL in different bacterial groups, supporting enormous functional and structural plasticity for this molecule and the existence of a hidden combinatorial code in the protein sequence enabling such functions. Describing this plasticity can shed light on the functional diversity of GroEL. We hypothesize that different overlapping sets of amino acids coevolve within GroEL, GroES and between both these proteins. Shifts in these coevolutionary relationships may inevitably lead to evolution of alternative functions.ResultsWe conducted the first coevolution analyses in an extensive bacterial phylogeny, revealing complex networks of evolutionary dependencies between residues in GroESL. These networks differed among bacterial groups and involved amino acid sites with functional importance and others with previously unsuspected functional potential. Coevolutionary networks formed statistically independent units among bacterial groups and map to structurally continuous regions in the protein, suggesting their functional link. Sites involved in coevolution fell within narrow structural regions, supporting dynamic combinatorial functional links involving similar protein domains. Moreover, coevolving sites within a bacterial group mapped to regions previously identified as involved in folding-unrelated functions, and thus, coevolution may mediate alternative functions.ConclusionsOur results highlight the evolutionary plasticity of GroEL across the entire bacterial phylogeny. Evidence on the functional importance of coevolving sites illuminates the as yet unappreciated functional diversity of proteins.

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Characterisation of mutations in GroES that allow GroEL to function as a single ring

Cited by 17 publications

References 35 publications

Myxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroES

Myxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroES

Stimulating the Substrate Folding Activity of a Single Ring GroEL Variant by Modulating the Cochaperonin GroES

Coevolution analyses illuminate the dependencies between amino acid sites in the chaperonin system GroES-L

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