Eintrag weiter verarbeiten
Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis
Gespeichert in:
| Zeitschriftentitel: | Journal of Bacteriology |
|---|---|
| Personen und Körperschaften: | , |
| In: | Journal of Bacteriology, 189, 2007, 19, S. 6787-6795 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
Gold, Nicholas D. Martin, Vincent J. J. Gold, Nicholas D. Martin, Vincent J. J. |
|---|---|
| author |
Gold, Nicholas D. Martin, Vincent J. J. |
| spellingShingle |
Gold, Nicholas D. Martin, Vincent J. J. Journal of Bacteriology Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis Molecular Biology Microbiology |
| author_sort |
gold, nicholas d. |
| spelling |
Gold, Nicholas D. Martin, Vincent J. J. 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.00882-07 <jats:title>ABSTRACT</jats:title> <jats:p> A metabolic isotope-labeling strategy was used in conjunction with nano-liquid chromatography-electrospray ionization mass spectrometry peptide sequencing to assess quantitative alterations in the expression patterns of subunits within cellulosomes of the cellulolytic bacterium <jats:italic>Clostridium thermocellum</jats:italic> , grown on either cellulose or cellobiose. In total, 41 cellulosomal proteins were detected, including 36 type I dockerin-containing proteins, which count among them all but three of the known docking components and 16 new subunits. All differential expression data were normalized to the scaffoldin CipA such that protein per cellulosome was compared for growth between the two substrates. Proteins that exhibited higher expression in cellulosomes from cellulose-grown cells than in cellobiose-grown cells were the cell surface anchor protein OlpB, exoglucanases CelS and CelK, and the glycoside hydrolase family 9 (GH9) endoglucanase CelJ. Conversely, lower expression in cellulosomes from cells grown on cellulose than on cellobiose was observed for the GH8 endoglucanase CelA; GH5 endoglucanases CelB, CelE, CelG; and hemicellulases XynA, XynC, XynZ, and XghA. GH9 cellulases were the most abundant group of enzymes per CipA when cells were grown on cellulose, while hemicellulases were the most abundant group on cellobiose. The results support the existing theory that expression of scaffoldin-related proteins is coordinately regulated by a catabolite repression type of mechanism, as well as the prior observation that xylanase expression is subject to a growth rate-independent type of regulation. However, concerning transcriptional control of cellulases, which had also been previously shown to be subject to catabolite repression, a novel distinction was observed with respect to endoglucanases. </jats:p> Global View of the <i>Clostridium thermocellum</i> Cellulosome Revealed by Quantitative Proteomic Analysis Journal of Bacteriology |
| doi_str_mv |
10.1128/jb.00882-07 |
| facet_avail |
Online Free |
| finc_class_facet |
Biologie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qYi4wMDg4Mi0wNw |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qYi4wMDg4Mi0wNw |
| institution |
DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 |
| imprint |
American Society for Microbiology, 2007 |
| imprint_str_mv |
American Society for Microbiology, 2007 |
| issn |
1098-5530 0021-9193 |
| issn_str_mv |
1098-5530 0021-9193 |
| language |
English |
| mega_collection |
American Society for Microbiology (CrossRef) |
| match_str |
gold2007globalviewoftheclostridiumthermocellumcellulosomerevealedbyquantitativeproteomicanalysis |
| publishDateSort |
2007 |
| publisher |
American Society for Microbiology |
| recordtype |
ai |
| record_format |
ai |
| series |
Journal of Bacteriology |
| source_id |
49 |
| title |
Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis |
| title_unstemmed |
Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis |
| title_full |
Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis |
| title_fullStr |
Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis |
| title_full_unstemmed |
Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis |
| title_short |
Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis |
| title_sort |
global view of the
<i>clostridium thermocellum</i>
cellulosome revealed by quantitative proteomic analysis |
| topic |
Molecular Biology Microbiology |
| url |
http://dx.doi.org/10.1128/jb.00882-07 |
| publishDate |
2007 |
| physical |
6787-6795 |
| description |
<jats:title>ABSTRACT</jats:title>
<jats:p>
A metabolic isotope-labeling strategy was used in conjunction with nano-liquid chromatography-electrospray ionization mass spectrometry peptide sequencing to assess quantitative alterations in the expression patterns of subunits within cellulosomes of the cellulolytic bacterium
<jats:italic>Clostridium thermocellum</jats:italic>
, grown on either cellulose or cellobiose. In total, 41 cellulosomal proteins were detected, including 36 type I dockerin-containing proteins, which count among them all but three of the known docking components and 16 new subunits. All differential expression data were normalized to the scaffoldin CipA such that protein per cellulosome was compared for growth between the two substrates. Proteins that exhibited higher expression in cellulosomes from cellulose-grown cells than in cellobiose-grown cells were the cell surface anchor protein OlpB, exoglucanases CelS and CelK, and the glycoside hydrolase family 9 (GH9) endoglucanase CelJ. Conversely, lower expression in cellulosomes from cells grown on cellulose than on cellobiose was observed for the GH8 endoglucanase CelA; GH5 endoglucanases CelB, CelE, CelG; and hemicellulases XynA, XynC, XynZ, and XghA. GH9 cellulases were the most abundant group of enzymes per CipA when cells were grown on cellulose, while hemicellulases were the most abundant group on cellobiose. The results support the existing theory that expression of scaffoldin-related proteins is coordinately regulated by a catabolite repression type of mechanism, as well as the prior observation that xylanase expression is subject to a growth rate-independent type of regulation. However, concerning transcriptional control of cellulases, which had also been previously shown to be subject to catabolite repression, a novel distinction was observed with respect to endoglucanases.
</jats:p> |
| container_issue |
19 |
| container_start_page |
6787 |
| container_title |
Journal of Bacteriology |
| container_volume |
189 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792344330392829957 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T17:05:32.131Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Global+View+of+the++++++++++++Clostridium+thermocellum++++++++++++Cellulosome+Revealed+by+Quantitative+Proteomic+Analysis&rft.date=2007-10-01&genre=article&issn=1098-5530&volume=189&issue=19&spage=6787&epage=6795&pages=6787-6795&jtitle=Journal+of+Bacteriology&atitle=Global+View+of+the%0A++++++++++++%3Ci%3EClostridium+thermocellum%3C%2Fi%3E%0A++++++++++++Cellulosome+Revealed+by+Quantitative+Proteomic+Analysis&aulast=Martin&aufirst=Vincent+J.+J.&rft_id=info%3Adoi%2F10.1128%2Fjb.00882-07&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792344330392829957 |
| author | Gold, Nicholas D., Martin, Vincent J. J. |
| author_facet | Gold, Nicholas D., Martin, Vincent J. J., Gold, Nicholas D., Martin, Vincent J. J. |
| author_sort | gold, nicholas d. |
| container_issue | 19 |
| container_start_page | 6787 |
| container_title | Journal of Bacteriology |
| container_volume | 189 |
| description | <jats:title>ABSTRACT</jats:title> <jats:p> A metabolic isotope-labeling strategy was used in conjunction with nano-liquid chromatography-electrospray ionization mass spectrometry peptide sequencing to assess quantitative alterations in the expression patterns of subunits within cellulosomes of the cellulolytic bacterium <jats:italic>Clostridium thermocellum</jats:italic> , grown on either cellulose or cellobiose. In total, 41 cellulosomal proteins were detected, including 36 type I dockerin-containing proteins, which count among them all but three of the known docking components and 16 new subunits. All differential expression data were normalized to the scaffoldin CipA such that protein per cellulosome was compared for growth between the two substrates. Proteins that exhibited higher expression in cellulosomes from cellulose-grown cells than in cellobiose-grown cells were the cell surface anchor protein OlpB, exoglucanases CelS and CelK, and the glycoside hydrolase family 9 (GH9) endoglucanase CelJ. Conversely, lower expression in cellulosomes from cells grown on cellulose than on cellobiose was observed for the GH8 endoglucanase CelA; GH5 endoglucanases CelB, CelE, CelG; and hemicellulases XynA, XynC, XynZ, and XghA. GH9 cellulases were the most abundant group of enzymes per CipA when cells were grown on cellulose, while hemicellulases were the most abundant group on cellobiose. The results support the existing theory that expression of scaffoldin-related proteins is coordinately regulated by a catabolite repression type of mechanism, as well as the prior observation that xylanase expression is subject to a growth rate-independent type of regulation. However, concerning transcriptional control of cellulases, which had also been previously shown to be subject to catabolite repression, a novel distinction was observed with respect to endoglucanases. </jats:p> |
| doi_str_mv | 10.1128/jb.00882-07 |
| facet_avail | Online, Free |
| finc_class_facet | Biologie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qYi4wMDg4Mi0wNw |
| imprint | American Society for Microbiology, 2007 |
| imprint_str_mv | American Society for Microbiology, 2007 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
| issn | 1098-5530, 0021-9193 |
| issn_str_mv | 1098-5530, 0021-9193 |
| language | English |
| last_indexed | 2024-03-01T17:05:32.131Z |
| match_str | gold2007globalviewoftheclostridiumthermocellumcellulosomerevealedbyquantitativeproteomicanalysis |
| mega_collection | American Society for Microbiology (CrossRef) |
| physical | 6787-6795 |
| publishDate | 2007 |
| publishDateSort | 2007 |
| publisher | American Society for Microbiology |
| record_format | ai |
| recordtype | ai |
| series | Journal of Bacteriology |
| source_id | 49 |
| spelling | Gold, Nicholas D. Martin, Vincent J. J. 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.00882-07 <jats:title>ABSTRACT</jats:title> <jats:p> A metabolic isotope-labeling strategy was used in conjunction with nano-liquid chromatography-electrospray ionization mass spectrometry peptide sequencing to assess quantitative alterations in the expression patterns of subunits within cellulosomes of the cellulolytic bacterium <jats:italic>Clostridium thermocellum</jats:italic> , grown on either cellulose or cellobiose. In total, 41 cellulosomal proteins were detected, including 36 type I dockerin-containing proteins, which count among them all but three of the known docking components and 16 new subunits. All differential expression data were normalized to the scaffoldin CipA such that protein per cellulosome was compared for growth between the two substrates. Proteins that exhibited higher expression in cellulosomes from cellulose-grown cells than in cellobiose-grown cells were the cell surface anchor protein OlpB, exoglucanases CelS and CelK, and the glycoside hydrolase family 9 (GH9) endoglucanase CelJ. Conversely, lower expression in cellulosomes from cells grown on cellulose than on cellobiose was observed for the GH8 endoglucanase CelA; GH5 endoglucanases CelB, CelE, CelG; and hemicellulases XynA, XynC, XynZ, and XghA. GH9 cellulases were the most abundant group of enzymes per CipA when cells were grown on cellulose, while hemicellulases were the most abundant group on cellobiose. The results support the existing theory that expression of scaffoldin-related proteins is coordinately regulated by a catabolite repression type of mechanism, as well as the prior observation that xylanase expression is subject to a growth rate-independent type of regulation. However, concerning transcriptional control of cellulases, which had also been previously shown to be subject to catabolite repression, a novel distinction was observed with respect to endoglucanases. </jats:p> Global View of the <i>Clostridium thermocellum</i> Cellulosome Revealed by Quantitative Proteomic Analysis Journal of Bacteriology |
| spellingShingle | Gold, Nicholas D., Martin, Vincent J. J., Journal of Bacteriology, Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis, Molecular Biology, Microbiology |
| title | Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis |
| title_full | Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis |
| title_fullStr | Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis |
| title_full_unstemmed | Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis |
| title_short | Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis |
| title_sort | global view of the <i>clostridium thermocellum</i> cellulosome revealed by quantitative proteomic analysis |
| title_unstemmed | Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis |
| topic | Molecular Biology, Microbiology |
| url | http://dx.doi.org/10.1128/jb.00882-07 |