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https://hdl.handle.net/2440/11269
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dc.contributor.author | Val, D. | - |
dc.contributor.author | Chapman-Smith, A. | - |
dc.contributor.author | Walker, M. | - |
dc.contributor.author | Cronan, J. | - |
dc.contributor.author | Wallace, J. | - |
dc.date.issued | 1995 | - |
dc.identifier.citation | Biochemical Journal, 1995; 312(3):817-825 | - |
dc.identifier.issn | 0264-6021 | - |
dc.identifier.issn | 1470-8728 | - |
dc.identifier.uri | http://hdl.handle.net/2440/11269 | - |
dc.description.abstract | In Saccharomyces cerevisiae there are two isoenzymes of pyruvate carboxylase (Pyc) encoded by separate genes designated PYC1 and PYC2. We report the isolation and sequencing of a PYC2 gene, and the localization of both genes on the physical map of S. cerevisiae. Comparison with the previously reported sequence [Stucka, Dequin, Salmon and Gancedo (1991) Mol. Gen. Genet. 229, 307-315] revealed significant differences within the open reading frame. The most notable difference was near the 3' end, where we found a single base deletion reducing the open reading frame by 15 bases. We have confirmed the C-terminus of Pyc2 encoded by the gene isolated here by expressing and purifying an 86-amino-acid biotin-domain peptide. In addition, we investigated the effects of the two changes in the Pyc2 biotin domain (K1155R substitution and Q1178P/five-amino-acid extension) on the extent of biotinylation in vivo by Escherichia coli biotin ligase, and compared the biotinylation of peptides containing these changes with that of two different-length Pyc1 biotin-domain peptides. The K1155R substitution had very little effect on biotinylation, but the five-amino-acid C-terminal extension to Pyc2 and the N-terminal extension to Pycl both improved biotinylation in vivo. | - |
dc.language.iso | en | - |
dc.publisher | The Biochemical Society, London | - |
dc.source.uri | http://dx.doi.org/10.1042/bj3120817 | - |
dc.subject | Escherichia coli | - |
dc.subject | Saccharomyces cerevisiae | - |
dc.subject | Biotin | - |
dc.subject | Isoenzymes | - |
dc.subject | Pyruvate Carboxylase | - |
dc.subject | DNA, Fungal | - |
dc.subject | Chromosome Mapping | - |
dc.subject | Sequence Analysis | - |
dc.subject | Mutagenesis | - |
dc.subject | Binding Sites | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Base Sequence | - |
dc.subject | Sequence Homology | - |
dc.subject | Polymorphism, Genetic | - |
dc.subject | Genes, Fungal | - |
dc.subject | Molecular Sequence Data | - |
dc.title | Polymorphism of the yeast pyruvate carboxylase 2 gene and protein: Effects on biotinylation | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1042/bj3120817 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Walker, M. [0000-0002-6934-3787] | - |
Appears in Collections: | Aurora harvest 2 Biochemistry publications |
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