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Brief Communication 1053 Recurrent paralogy in the evolution of archaeal chaperonins
 

Summary: Brief Communication 1053
Recurrent paralogy in the evolution of archaeal chaperonins
John M. Archibald, John M. Logsdon Jr and W. Ford Doolittle
Chaperonins are multisubunit double-ring complexes
that mediate the folding of nascent proteins [1,2]. In
bacteria, chaperonins are homo-oligomeric and are
composed of seven-membered rings. Eukaryotic and
most archaeal chaperonin rings are eight-membered
and exhibit varying degrees of hetero-oligomerism
[3,4]. We have cloned and sequenced seven new genes
encoding chaperonin subunits from the crenarchaeotes
Sulfolobus solfataricus, S. acidocaldarius, S. shibatae
and Desulfurococcus mobilis. Although some archaeal
genomes possess a single chaperonin gene, most have
two. We describe a third chaperonin-encoding gene
(TF55-) from two Sulfolobus species; phylogenetic
analyses indicate that the gene duplication producing
TF55- occurred within crenarchaeal evolution. The
presence of TF55- in Sulfolobus correlates with their
unique nine-membered chaperonin rings. Duplicate

  

Source: Archibald, John - Department of Biochemistry and Molecular Biology, Dalhousie University

 

Collections: Biology and Medicine