MCHUGH, C.A., J. FONTANA, Daniel NĚMEČEK, N.Q. CHENG, A.A. AKSYUK, J.B. HEYMANN, D.C. WINKLER, A.S. LAM, J.S. WALL, A.C. STEVEN and E. HOICZYK. A virus capsid-like nanocompartment that stores iron and protects bacteria from oxidative stress. EMBO Journal. HOBOKEN: WILEY-BLACKWELL, 2014, vol. 33, No 17, p. 1896-1911. ISSN 0261-4189. Available from: https://dx.doi.org/10.15252/embj.201488566.
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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
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 10.434
RIV identification code RIV/00216224:14740/14:00079216
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.15252/embj.201488566
UT WoS 000341839500008
Keywords in English cryo-electron microscopy; encapsulin; ferritin; HK97 fold; oxidative stress
Tags kontrola MP, MP, rivok, SCOPUS
Tags International impact, Reviewed
Changed by Changed by: Martina Prášilová, učo 342282. Changed: 10/3/2015 14:43.
Abstract
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.
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