In:
FEBS Letters, Wiley, Vol. 414, No. 1 ( 1997-09), p. 95-98
Abstract:
Following in vitro translation of the 22 kDa peroxisomal membrane protein (Pmp22p), gel filtration analysis of the post‐ribosomal supernatant revealed that Pmp22p forms two complexes. Complex I is of high molecular weight, results in a crosslinking product of 80 kDa, and by co‐immunoprecipitation with anti‐TCP1 antibody was identified as TRiC. In complex II Pmp22p was crosslinked to a yet unknown polypeptide of 40 kDa (P 40). This complex exhibited much higher efficiency to insert Pmp22p into the peroxisomal membrane compared to complex I. In a model we suggest that newly synthesized Pmp22p is first bound to TRiC before being transferred to P 40 which may function as a cytosolic Pmp22p receptor.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(97)00975-7
Language:
English
Publisher:
Wiley
Publication Date:
1997
detail.hit.zdb_id:
1460391-3
SSG:
12
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