J 2014

A virus capsid-like nanocompartment that stores iron and protects bacteria from oxidative stress

MCHUGH, C.A., J. FONTANA, Daniel NĚMEČEK, N.Q. CHENG, A.A. AKSYUK et. al.

Basic information

Original name

A virus capsid-like nanocompartment that stores iron and protects bacteria from oxidative stress

Authors

MCHUGH, C.A. (840 United States of America), J. FONTANA (840 United States of America), Daniel NĚMEČEK (203 Czech Republic, guarantor, belonging to the institution), N.Q. CHENG (840 United States of America), A.A. AKSYUK (840 United States of America), J.B. HEYMANN (840 United States of America), D.C. WINKLER (840 United States of America), A.S. LAM (840 United States of America), J.S. WALL (840 United States of America), A.C. STEVEN (840 United States of America) and E. HOICZYK (840 United States of America)

Edition

EMBO Journal, HOBOKEN, WILEY-BLACKWELL, 2014, 0261-4189

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

Impact factor

Impact factor: 10.434

RIV identification code

RIV/00216224:14740/14:00079216

Organization unit

Central European Institute of Technology

UT WoS

000341839500008

Keywords in English

cryo-electron microscopy; encapsulin; ferritin; HK97 fold; oxidative stress

Tags

International impact, Reviewed
Změněno: 10/3/2015 14:43, Martina Prášilová

Abstract

V originále

Living cells compartmentalize materials and enzymatic reactions to increase metabolic efficiency. While eukaryotes use membrane-bound organelles, bacteria and archaea rely primarily on protein-bound nanocompartments. Encapsulins constitute a class of nanocompartments widespread in bacteria and archaea whose functions have hitherto been unclear. Here, we characterize the encapsulin nanocompartment from Myxococcus xanthus, which consists of a shell protein (EncA, 32.5 kDa) and three internal proteins (EncB, 17 kDa; EncC, 13 kDa; EncD, 11 kDa). Using cryo-electron microscopy, we determined that EncA self-assembles into an icosahedral shell 32 nm in diameter (26 nm internal diameter), built from 180 subunits with the fold first observed in bacteriophage HK97 capsid. The internal proteins, of which EncB and EncC have ferritin-like domains, attach to its inner surface. Native nanocompartments have dense iron-rich cores. Functionally, they resemble ferritins, cage-like iron storage proteins, but with a massively greater capacity (similar to 30,000 iron atoms versus similar to 3,000 in ferritin). Physiological data reveal that few nanocompartments are assembled during vegetative growth, but they increase fivefold upon starvation, protecting cells from oxidative stress through iron sequestration.