![Sample our Bioscience journals, sign in here to start your access, Latest two full volumes FREE to you for 14 days]({"type":"image" , "src" : "/sda/5925/TOC-Subject-Sample-2021-Bioscience.jpg"})
Abstract
A cDNA sequence encoding a chaperone protein from bovine heart mitochondria is described. It is deduced from overlapping partial cDNAs amplified in polymerase chain reactions from bovine heart cDNA, using in the first instance mixtures of synthetic oligonucleotide primers based on the incomplete sequence of the cpn10 (Hsp10) chaperone protein from rat liver mitochondria. The encoded bovine protein sequence is 101 amino acids in length. By analogy with the rat homologue it is likely that the initiator methionine is removed after translation and that the mature N-terminal is modified. The mitochondrial proteins are members of the chaperonin 10 family which also includes the bacterial GroES chaperones. These proteins act in conjunction with members of the chaperonin-60 protein family, such as bacterial GroEL, to facilitate the folding of newly syn-thesised or translocated proteins.