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Title: Purification and characterization of DR_2577 (SlpA) a major S-layer protein from Deinococcus radiodurans

The protein DR_2577 is a major Surface layer component of the radio-resistant bacterium Deinococcus radiodurans. In the present study DR_2577 has been purified and its oligomeric profile characterized by means of size exclusion chromatography and gel electrophoresis. DR_2577 was found to be organized into three hierarchical orders characterized by monomers, stable dimers formed by the occurrence of disulfide bonds, and hexamers resulting from a combination of dimers. Finally, the structural implications of these findings are discussed providing new elements for a more integrated model of this S-layer.
Authors:
 [1] ;  [2] ;  [1] ;  [3] ;  [1] ;  [4]
  1. Univ. of Cagliari, Cagliari (Italy)
  2. European Molecular Biology Lab. (EMBL), Grenoble (France); Univ. Grenoble, Grenoble (France). Alpes-EMBL-National Center for Scientific Research
  3. Brookhaven National Lab. (BNL), Upton, NY (United States). Dept. of Photon Sciences
  4. Univ. of Cagliari, Cagliari (Italy); International Institute of Molecular and Cell Biology, Warsaw (Poland)
Publication Date:
Report Number(s):
BNL-111379-2015-JA
Journal ID: ISSN 1664-302X
Grant/Contract Number:
SC00112704
Type:
Accepted Manuscript
Journal Name:
Frontiers in Microbiology
Additional Journal Information:
Journal Volume: 6; Journal ID: ISSN 1664-302X
Publisher:
Frontiers Research Foundation
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; S-layer; hexagonally packed intermediate; SlpA; DR_2577; Deinococcus radiodurans
OSTI Identifier:
1229304

Farci, Domenica, Bowler, Matthew W., Esposito, Francesca, McSweeney, Sean, Tramontano, Enzo, and Piano, Dario. Purification and characterization of DR_2577 (SlpA) a major S-layer protein from Deinococcus radiodurans. United States: N. p., Web. doi:10.3389/fmicb.2015.00414.
Farci, Domenica, Bowler, Matthew W., Esposito, Francesca, McSweeney, Sean, Tramontano, Enzo, & Piano, Dario. Purification and characterization of DR_2577 (SlpA) a major S-layer protein from Deinococcus radiodurans. United States. doi:10.3389/fmicb.2015.00414.
Farci, Domenica, Bowler, Matthew W., Esposito, Francesca, McSweeney, Sean, Tramontano, Enzo, and Piano, Dario. 2015. "Purification and characterization of DR_2577 (SlpA) a major S-layer protein from Deinococcus radiodurans". United States. doi:10.3389/fmicb.2015.00414. https://www.osti.gov/servlets/purl/1229304.
@article{osti_1229304,
title = {Purification and characterization of DR_2577 (SlpA) a major S-layer protein from Deinococcus radiodurans},
author = {Farci, Domenica and Bowler, Matthew W. and Esposito, Francesca and McSweeney, Sean and Tramontano, Enzo and Piano, Dario},
abstractNote = {The protein DR_2577 is a major Surface layer component of the radio-resistant bacterium Deinococcus radiodurans. In the present study DR_2577 has been purified and its oligomeric profile characterized by means of size exclusion chromatography and gel electrophoresis. DR_2577 was found to be organized into three hierarchical orders characterized by monomers, stable dimers formed by the occurrence of disulfide bonds, and hexamers resulting from a combination of dimers. Finally, the structural implications of these findings are discussed providing new elements for a more integrated model of this S-layer.},
doi = {10.3389/fmicb.2015.00414},
journal = {Frontiers in Microbiology},
number = ,
volume = 6,
place = {United States},
year = {2015},
month = {6}
}