Local Variability of the Phosphoglycerate Kinase-Triosephosphate Isomerase Fusion Protein from Thermotoga maritima MSB 8
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Doris Wassenberg
Abstract
The pgktpi gene locus of Thermotoga maritima 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 frameshift 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 al., EMBO J. 14 (1995), 442 451]. Surprisingly, the complete T. maritima genome was found to contain a pgktpi 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 pgktpi 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.
Copyright © 2001 by Walter de Gruyter GmbH & Co. KG
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- Revealing the Potential of DNA-Based Vaccination: Lessons Learned from the Hepatitis B Virus Surface Antigen
- Progress toward a Malaria Vaccine: Efficient Induction of Protective Anti-Malaria Immunity
- Peptide Vaccines and Peptide Libraries
- Defined Synthetic Vaccines
- Antimicrobial Peptides: Properties and Applicability
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- The Role of Heat Shock Proteins and Their Receptors in the Activation of the Immune System
- Transcriptional Repression Mediated by the KRAB Domain of the Human C2H2 Zinc Finger Protein Kox1/ZNF10 Does Not Require Histone Deacetylation
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