NON-CLATHRIN-COAT PROTEIN-ALPHA IS A CONSERVED SUBUNIT OF COATOMER AND IN SACCHAROMYCES-CEREVISIAE IS ESSENTIAL FOR GROWTH

被引：55
作者：
GERICH, B
ORCI, L
TSCHOCHNER, H
LOTTSPEICH, F
RAVAZZOLA, M
AMHERDT, M
WIELAND, F
HARTER, C
机构：
[1] MAX PLANCK INST BIOCHEM, GENZENTRUM, D-82152 MARTINSRIED, GERMANY
[2] UNIV GENEVA, SCH MED, DEPT MORPHOL, CH-1211 GENEVA 4, SWITZERLAND
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 08期
关键词：
SECRETORY PATHWAY; COAT PROTEIN-COATED VESICLES; GOLGI MEMBRANES; WD-40; REPEAT;
D O I：
10.1073/pnas.92.8.3229
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
To complete the molecular characterization of coatomer, the preformed cytosolic complex that is involved in the formation of biosynthetic transport vesicles, we have cloned and characterized the gene for non clathrin-coat protein alpha (alpha-COP) from Saccharomyces cerevisiae. The derived protein, molecular weight of 135,500, contains four WD-40 repeated motifs (Trp/Asp-containing motifs of approximate to 40 amino acids). Disruption of the yeast alpha-COP gene is lethal. Comparison of the DNA-derived primary structure with peptides from bovine alpha-COP shows a striking homology. alpha-COP is localized to coated transport vesicles and coated buds of Golgi membranes derived from CHO cells.
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收藏
页码：3229 / 3233
页数：5
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