Detailed Information on Publication Record
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
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.