| First Author | Xie X | Year | 1994 |
| Journal | Blood | Volume | 84 |
| Issue | 7 | Pages | 2171-4 |
| PubMed ID | 7919332 | Mgi Jnum | J:20653 |
| Mgi Id | MGI:68729 | Doi | 10.1182/blood.v84.7.2171.2171 |
| Citation | Xie X, et al. (1994) Cloning and expression of a new mammalian chaperonin gene from a multipotent hematopoietic progenitor clone. Blood 84(7):2171-4 |
| abstractText | 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. |
