Proteome Analyses of Hydrogen-producing Hyperthermophilic Archaeon Thermococcus onnurineus NA1 in Different One-carbon Substrate Culture Conditions SCIE SCOPUS

DC Field Value Language
dc.contributor.author Moon, Yoon-Jung -
dc.contributor.author Kwon, Joseph -
dc.contributor.author Yun, Sung-Ho -
dc.contributor.author Lim, Hye Li -
dc.contributor.author Kim, Min-Sik -
dc.contributor.author Kang, Sung Gyun -
dc.contributor.author Lee, Jung-Hyun -
dc.contributor.author Choi, Jong-Soon -
dc.contributor.author Kim, Seung Il -
dc.contributor.author Chung, Young-Ho -
dc.date.accessioned 2020-04-20T06:55:15Z -
dc.date.available 2020-04-20T06:55:15Z -
dc.date.created 2020-01-28 -
dc.date.issued 2012-06 -
dc.identifier.issn 1535-9476 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/3587 -
dc.description.abstract Thermococcus onnurineus NA1, a sulfur-reducing hyperthermophilic archaeon, is capable of H-2-producing growth, considered to be hydrogenogenic carboxydotrophy. Utilization of formate as a sole energy source has been well studied in T. onnurineus NA1. However, whether formate can be used as its carbon source remains unknown. To obtain a global view of the metabolic characteristics of H-2-producing growth, a quantitative proteome analysis of T. onnurineus NA1 grown on formate, CO, and starch was performed by combining one-dimensional SDS-PAGE with nano UPLC-MSE. A total of 587 proteins corresponding to 29.7% of the encoding genes were identified, and the major metabolic pathways (especially energy metabolism) were characterized at the protein level. Expression of glycolytic enzymes was common but more highly induced in starch-grown cells. In contrast, enzymes involved in key steps of the gluconeogenesis and pentose phosphate pathways were strongly up-regulated in formate-grown cells, suggesting that formate could be utilized as a carbon source by T. onnurineus NA1. In accordance with the genomic analysis, comprehensive proteomic analysis also revealed a number of hydrogenase clusters apparently associated with formate metabolism. On the other hand, CODH and CO-induced hydrogenases belonging to the Hyg4-II cluster, as well as sulfhydrogenase-I and Mbx, were prominently expressed during CO culture. Our data suggest that CO can be utilized as a sole energy source for H-2 production via an electron transport mechanism and that CO2 produced from catabolism or CO oxidation by CODH and CO-induced hydrogenases may subsequently be assimilated into the organic carbon. Overall, proteomic comparison of formate-and CO-grown cells with starch-grown cells revealed that a single carbon compound, such as formate and CO, can be utilized as an efficient substrate to provide cellular carbon and/or energy by T. onnurineus NA1. Molecular & Cellular Proteomics 11: 10.1074/mcp.M111.015420, 1-15, 2012. -
dc.description.uri 1 -
dc.language English -
dc.publisher AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC -
dc.subject PYRUVATE-FERREDOXIN OXIDOREDUCTASE -
dc.subject COMPLETE GENOME SEQUENCE -
dc.subject SEA HYDROTHERMAL VENT -
dc.subject RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE -
dc.subject PYROCOCCUS-FURIOSUS -
dc.subject H-2 PRODUCTION -
dc.subject CO OXIDATION -
dc.subject CARBOXYDOTHERMUS HYDROGENOFORMANS -
dc.subject METHANOBACTERIUM-FORMICICUM -
dc.subject DEOXYRIBONUCLEIC ACID -
dc.title Proteome Analyses of Hydrogen-producing Hyperthermophilic Archaeon Thermococcus onnurineus NA1 in Different One-carbon Substrate Culture Conditions -
dc.type Article -
dc.citation.title MOLECULAR & CELLULAR PROTEOMICS -
dc.citation.volume 11 -
dc.citation.number 6 -
dc.contributor.alternativeName 김민식 -
dc.contributor.alternativeName 강성균 -
dc.contributor.alternativeName 이정현 -
dc.identifier.bibliographicCitation MOLECULAR & CELLULAR PROTEOMICS, v.11, no.6 -
dc.identifier.doi 10.1074/mcp.M111.015420 -
dc.identifier.scopusid 2-s2.0-84862336123 -
dc.identifier.wosid 000306408500010 -
dc.type.docType Article -
dc.description.journalClass 1 -
dc.subject.keywordPlus PYRUVATE-FERREDOXIN OXIDOREDUCTASE -
dc.subject.keywordPlus COMPLETE GENOME SEQUENCE -
dc.subject.keywordPlus SEA HYDROTHERMAL VENT -
dc.subject.keywordPlus RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE -
dc.subject.keywordPlus PYROCOCCUS-FURIOSUS -
dc.subject.keywordPlus H-2 PRODUCTION -
dc.subject.keywordPlus CO OXIDATION -
dc.subject.keywordPlus CARBOXYDOTHERMUS HYDROGENOFORMANS -
dc.subject.keywordPlus METHANOBACTERIUM-FORMICICUM -
dc.subject.keywordPlus DEOXYRIBONUCLEIC ACID -
dc.relation.journalWebOfScienceCategory Biochemical Research Methods -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.relation.journalResearchArea Biochemistry & Molecular Biology -
Appears in Collections:
Marine Resources Research Division > Marine Biotechnology Research Center > 1. Journal Articles
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