The ntp operon encoding the Na+ V-ATPase of the thermophile Caloramator fervidus
| Autor: | Jeroen G. Nijland, Trees Ubbink-Kok, Dirk Jan Slotboom, Juke S. Lolkema |
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| Přispěvatelé: | Groningen Biomolecular Sciences and Biotechnology, Molecular Microbiology, Enzymology, Faculty of Science and Engineering |
| Rok vydání: | 2006 |
| Předmět: |
Gram-Positive Endospore-Forming Rods
Vacuolar Proton-Translocating ATPases Enzyme complex SUBUNIT ARRANGEMENT Operon ATPase Molecular Sequence Data V-ATPase ntp Operon Biochemistry Microbiology central stalk ENTEROCOCCUS-HIRAE STATOR STRUCTURE Genetics Amino Acid Sequence Molecular Biology ELECTRON-MICROSCOPY chemistry.chemical_classification thermophile COMPLEX PURIFICATION biology Thermophile Structural gene Caloramator fervidus V-TYPE ATPASE Nucleic acid sequence BACTERIUM CLOSTRIDIUM FERVIDUS General Medicine Thermus thermophilus biology.organism_classification molecular motor Enzyme chemistry Multiprotein Complexes THERMUS-THERMOPHILUS biology.protein Electrophoresis Polyacrylamide Gel PERIPHERAL STALK Sodium-Potassium-Exchanging ATPase |
| Zdroj: | Archives of Microbiology, 186(6), 513-517. SPRINGER |
| ISSN: | 1432-072X 0302-8933 |
| DOI: | 10.1007/s00203-006-0165-x |
| Popis: | The V-type ATPase of the thermophile Caloramator fervidus is an ATP-driven Na+ pump. The nucleotide sequence of the ntpFIKECGABD operon containing the structural genes coding for the nine subunits of the enzyme complex was determined. The identity of the proteins in two pairs of subunits (D, E and F, G) that have very similar mobilities on SDS-PAGE of the purified complex (24.3 and 22.7 kDa, and 12.3 and 11.6 kDa) was established by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides. |
| Databáze: | OpenAIRE |
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