STRUCTURE OF HOLO-CHAPERONIN STUDIED WITH ELECTRON-MICROSCOPY - OLIGOMERIC CPN 10 ON TOP OF 2 LAYERS OF CPN60 RINGS WITH 2 STRIPES EACH

被引：72

作者：

ISHII, N ^{[1
]}

TAGUCHI, H ^{[1
]}

SUMI, M ^{[1
]}

YOSHIDA, M ^{[1
]}

机构：

[1] TOKYO INST TECHNOL,DEPT LIFE SCI,RESOURCES UTILIZAT LAB R1,NAGATSUTA 4259,YOKOHAMA,KANAGAWA 227,JAPAN

来源：

FEBS LETTERS | 1992年 / 299卷 / 02期

关键词：

CHAPERONIN; HOLO-CHAPERONIN; ELECTRON MICROSCOPY; THERMUS-THERMOPHILUS;

D O I：

10.1016/0014-5793(92)80240-H

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A structural model of holo-chaperonin, known as a protein-folding control protein comprising 60 kDa (cpn60) and 10 kDa polypeptides (cpn10), is proposed based on the electron microscopic images of holo-chaperonin from Thermus thermophilus and cpn60 from Paracoccus denitrificans. Isolated Paracoccus cpn60 shows very similar images to those of Escherichia coli tetradecameric cpn60, a seven-membered ring in the top view and a rectangular shape with four stripes in the side view. However, a small number of half-thick rectangles with two stripes are also seen which indicates that a single cpn60-heptamer ring has two stripes parallel to the plane of the ring. Thermus holo-chaperonin shows a bullet-like shape in the side view, and antibody against cpn10 binds only to the round side of the bullet. We conclude that a single cpn60-heptamer ring with two stripes stacks into two layers, and a cpn10 oligomer binds to one side of the layers.

引用

页码：169 / 174

页数：6

共 26 条

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