Wassenberg, Doris and Wuhrer, Manfred and Beaucamp, Nicola and Schurig, Hartmut and Wozny, Manfred and Reusch, Dietmar and Fabry, Stefan and Jaenicke, Rainer (2001) Local variability of the phosphoglycerate kinase-triosephosphate isomerase fusion protein from Thermotoga maritima MSB 8. BIOLOGICAL CHEMISTRY, 382 (4). pp. 693-697. ISSN 1431-6730
Full text not available from this repository.Abstract
The pgk-tpi gene locus of Thermotoga maritime encodes both phosphoglycerate kinase (PGK) and a bienzyme complex consisting of a fusion protein of PGK with triosephosphate isomerase (TIM). No separate tpi gene for TIM is present in T. maritima. A frame-shift at the end of the pgk gene has been previously proposed as a mechanism to regulate the expression of the two protein variants [Schurig et at, EMBO J. 14 (1995), 442-451]. Surprisingly, the complete T. maritima genome was found to contain a pgk-tpi sequence not requiring the proposed frameshift mechanism. To clarify the apparent discrepancy, a variety of DNA sequencing techniques were applied, disclosing an anomalous local variability in the pgk-tpi fusion region. The comparison of different DNA samples and the mass spectrometric analysis of the amino acid sequence of the natural fusion protein from T. maritima MSB8 confirmed the local variability of the DNA variants. Since not all peptide masses could be assigned, further variations are conceivable, suggesting an even higher heterogeneity of the T. maritima MSB8 strain.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | 3-PHOSPHOGLYCERATE KINASE; TRANSCRIPTIONAL SLIPPAGE; POLYACRYLAMIDE GELS; MASS-SPECTROMETRY; GENE; DISSECTION; STABILITY; GENOME; ENZYME; TIM; DE-MALDI-TOF; frameshift; mass spectrometry; PGK-TIM fusion protein; Thermotoga maritima |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 07 Feb 2022 06:36 |
| Last Modified: | 07 Feb 2022 06:36 |
| URI: | https://pred.uni-regensburg.de/id/eprint/41520 |
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