Proteomic analysis of cold adaptation in a Siberian permafrost bacterium – Exiguobacterium sibiricum 255–15 by two-dimensional liquid separation coupled with mass spectrometry
dc.contributor.author | Qiu, Yinghua | en_US |
dc.contributor.author | Kathariou, Sophia | en_US |
dc.contributor.author | Lubman, David M. | en_US |
dc.date.accessioned | 2007-09-20T17:47:02Z | |
dc.date.available | 2008-01-03T16:20:39Z | en_US |
dc.date.issued | 2006-10 | en_US |
dc.identifier.citation | Qiu, Yinghua; Kathariou, Sophia; Lubman, David M. (2006). "Proteomic analysis of cold adaptation in a Siberian permafrost bacterium – Exiguobacterium sibiricum 255–15 by two-dimensional liquid separation coupled with mass spectrometry." PROTEOMICS 6(19): 5221-5233. <http://hdl.handle.net/2027.42/55850> | en_US |
dc.identifier.issn | 1615-9853 | en_US |
dc.identifier.issn | 1615-9861 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/55850 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=16955517&dopt=citation | en_US |
dc.description.abstract | Bacterial cold adaptation in Exiguobacterium sibiricum 255–15 was studied on a proteomic scale using a 2-D liquid phase separation coupled with MS technology. Whole-cell lysates of E. sibiricum 255–15 grown at 4°C and 25°C were first fractionated according to p I by chromatofocusing (CF), and further separated based on hydrophobicity by nonporous silica RP HPLC (NPS-RP-HPLC) which was on-line coupled with an ESI-TOF MS for intact protein M r measurement and quantitative interlysate comparison. Mass maps were created to visualize the differences in protein expression between different growth temperatures. The differentially expressed proteins were then identified by PMF using a MALDI-TOF MS and peptide sequencing by MS/MS with a MALDI quadrupole IT TOF mass spectrometer (MALDI-QIT-TOF MS). A total of over 500 proteins were detected in this study, of which 256 were identified. Among these proteins 39 were cold acclimation proteins (Caps) that were preferentially or uniquely expressed at 4°C and three were homologous cold shock proteins (Csps). The homologous Csps were found to be similarly expressed at 4°C and 25°C, where these three homologous Csps represent about 10% of the total soluble proteins at both 4°C and 25°C. | en_US |
dc.format.extent | 345578 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | WILEY-VCH Verlag | en_US |
dc.subject.other | Life and Medical Sciences | en_US |
dc.title | Proteomic analysis of cold adaptation in a Siberian permafrost bacterium – Exiguobacterium sibiricum 255–15 by two-dimensional liquid separation coupled with mass spectrometry | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, MI, USA ; Department of Surgery, University of Michigan Medical Center, Ann Arbor, MI, USA ; University of Michigan, Department of Surgery, MSRB1 RmA510B, 1150 West Medical Center Drive, Ann Arbor, MI 48109, USA Fax: +1-734-760-6199 | en_US |
dc.contributor.affiliationother | Department of the Food Science, North Carolina State University, Raleigh, NC, USA | en_US |
dc.identifier.pmid | 16955517 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/55850/1/5221_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/pmic.200600071 | en_US |
dc.identifier.source | PROTEOMICS | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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