Cloning and expression of Xenopus CCT gamma, a chaperonin subunit developmentally regulated in neural-derived and myogenic lineages.
The chaperonin containing TCP-1 (CCT) is a eukaryotic cytoplasmic chaperonin, consisting of multiple distinct subunits in a double-toroid structure. In vitro, the CCT has been shown to assist in the folding of tubulin and actin into active conformations through an ATP-dependent mechanism. The function and distribution of these proteins in vivo are also not known. In this report, we show that the expression of two CCT subunits (alpha and gamma) are developmentally regulated in neural-derived and myogenic lineages. While expression in the central nervous system and muscle is consistent with a role in tubulin and actin conformation, we also detect robust expression in the developing cranial neural crest. Enrichment in the neural crest may represent the presence of a novel substrate for the CCT. We have also cloned the complete cDNA for the Xenopus ortholog of CCT gamma, which has 87% amino acid identity with the mouse protein. This remarkable evolutionary conservation suggests a conserved function for this protein among vertebrates, and possibly among all eukaryotes.
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins / Q000235:genetics*; D003001:Cloning, Molecular; D015870:Gene Expression; D051379:Mice; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides; D012333:RNA, Messenger; D017386:Sequence Homology, Amino Acid; D014982:Xenopus laevis / Q000196:embryology*
C533311:Cct3 protein, mouse; D009838:Oligodeoxyribonucleotides; D012333:RNA, Messenger; C533315:Tcp1 protein, mouse; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins