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X Xie and R Palacios
Department of Immunology, University of Texas M.D. Anderson Cancer Center,
Houston 77030.
Molecular chaperones assist in the folding and assembly of proteins in
cells. Although chaperonins have been shown in prokaryotes, mitochondria,
and chloroplasts long-ago, a cytoplasmic heteromeric chaperonin complex was
isolated only recently and found to contain at least five to six
polypeptides, one of which was identified as the product of the T complex
polypeptide-1 (TCP-1) gene. We have isolated and cloned a novel gene called
A45 from a cDNA library constructed from poly (A)+ RNA of a multipotent
hematopoietic progenitor clone. The A45 cDNA encodes a predicted
polypeptide of M(r) 58,118 that exhibits 32% overall amino acid sequence
identity to TCP-1 and contains the putative adenosine triphosphate-binding
domain and two characteristic consensus regions that are conserved in all
chaperonins. The A45 gene is expressed in hematopoietic precursors cells at
a much higher level than in nonhematopoietic cells and tissues. We conclude
that A45 represents a new member of the mammalian chaperonins that is
involved in the folding and assembly of polypeptides.
This article has been cited by other articles:
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| Copyright © 1994 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||