Molecular genetic basis of allelic polymorphism in malate dehydrogenase (mdh) in natural populations of Escherichia coli and Salmonella enterica
In: Proceedings of the National Academy of Sciences of the United States of America, Jg. 91 (1994), Heft 4, S. 1280-1284
Online
academicJournal
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Zugriff:
Nucleotide sequences of the mdh gene encoding the metabolic enzyme malate dehydrogenase (MDH) were determined for 44 strains representing the major lineages of Escherichia coli and the eight subspecies of Salmonella enterica. Sequence diversity was four times greater in S. enterica than in E. coli, and in both species the rate of amino acid substitution was lower in the NAD+-binding domain than in the catalytic domain. Divergence of the mdh genes of the two species apparently has not involved excess nonsynonymous substitutions residting from the fixation of adaptive amino acid mutations. Allozyme analysis detected 57% of the distinctive amino acid sequences.
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Molecular genetic basis of allelic polymorphism in malate dehydrogenase (mdh) in natural populations of Escherichia coli and Salmonella enterica
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Autor/in / Beteiligte Person: | BOYD, E. F ; NELSON, K ; FU-SHENG, WANG ; WHITTAM, T. S ; SELANDER, R. K |
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Zeitschrift: | Proceedings of the National Academy of Sciences of the United States of America, Jg. 91 (1994), Heft 4, S. 1280-1284 |
Veröffentlichung: | Washington, DC: National Academy of Sciences of the United States of America, 1994 |
Medientyp: | academicJournal |
Umfang: | print, 45 ref |
ISSN: | 0027-8424 (print) |
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