Unknown

Dataset Information

0

Cytochrome c polymerization by successive domain swapping at the C-terminal helix.


ABSTRACT: Cytochrome c (cyt c) is a stable protein that functions in a monomeric state as an electron donor for cytochrome c oxidase. It is also released to the cytosol when permeabilization of the mitochondrial outer membrane occurs at the early stage of apoptosis. For nearly half a century, it has been known that cyt c forms polymers, but the polymerization mechanism remains unknown. We found that cyt c forms polymers by successive domain swapping, where the C-terminal helix is displaced from its original position in the monomer and Met-heme coordination is perturbed significantly. In the crystal structures of dimeric and trimeric cyt c, the C-terminal helices are replaced by the corresponding domain of other cyt c molecules and Met80 is dissociated from the heme. The solution structures of dimeric, trimeric, and tetrameric cyt c were linear based on small-angle X-ray scattering measurements, where the trimeric linear structure shifted toward the cyclic structure by addition of PEG and (NH(4))(2)HPO(4). The absorption and CD spectra of high-order oligomers (approximately 40 mer) were similar to those of dimeric and trimeric cyt c but different from those of monomeric cyt c. For dimeric, trimeric, and tetrameric cyt c, the DeltaH of the oligomer dissociation to monomers was estimated to be about -20 kcal/mol per protomer unit, where Met-heme coordination appears to contribute largely to DeltaH. The present results suggest that cyt c polymerization occurs by successive domain swapping, which may be a common mechanism of protein polymerization.

SUBMITTER: Hirota S 

PROVIDER: S-EPMC2919943 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

Cytochrome c polymerization by successive domain swapping at the C-terminal helix.

Hirota Shun S   Hattori Yoko Y   Nagao Satoshi S   Taketa Midori M   Komori Hirofumi H   Kamikubo Hironari H   Wang Zhonghua Z   Takahashi Isao I   Negi Shigeru S   Sugiura Yukio Y   Kataoka Mikio M   Higuchi Yoshiki Y  

Proceedings of the National Academy of Sciences of the United States of America 20100706 29


Cytochrome c (cyt c) is a stable protein that functions in a monomeric state as an electron donor for cytochrome c oxidase. It is also released to the cytosol when permeabilization of the mitochondrial outer membrane occurs at the early stage of apoptosis. For nearly half a century, it has been known that cyt c forms polymers, but the polymerization mechanism remains unknown. We found that cyt c forms polymers by successive domain swapping, where the C-terminal helix is displaced from its origin  ...[more]

Similar Datasets

| S-EPMC4390240 | biostudies-literature
| S-EPMC3795569 | biostudies-literature
| S-EPMC4672631 | biostudies-literature
| S-EPMC4738263 | biostudies-literature
| S-EPMC1171690 | biostudies-other
| S-EPMC7837137 | biostudies-literature
| S-EPMC4137731 | biostudies-literature
| S-EPMC8694786 | biostudies-literature
| S-EPMC3127930 | biostudies-literature
| S-EPMC4302195 | biostudies-literature