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Evolution of substrate specificity in a recipient's enzyme following horizontal gene transfer
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Noda-Garcia, Lianet, Camacho-Zarco, Aldo R., Medina-Ruíz, Sophía, Gaytán, Paul, Carrillo-Tripp, Mauricio, Fülöp, Vilmos and Barona-Gómez, Francisco (2013) Evolution of substrate specificity in a recipient's enzyme following horizontal gene transfer. Molecular Biology and Evolution, Volume 30 (Number 9). pp. 2024-2034. doi:10.1093/molbev/mst115 ISSN 0737-4038.
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Official URL: http://dx.doi.org/10.1093/molbev/mst115
Abstract
Despite the prominent role of horizontal gene transfer (HGT) in shaping bacterial metabolism, little is known about the impact of HGT on the evolution of enzyme function. Specifically, what is the influence of a recently acquired gene on the function of an existing gene? For example, certain members of the genus Corynebacterium have horizontally acquired a whole L-tryptophan biosynthetic operon, whereas in certain closely related actinobacteria, for example, Mycobacterium, the trpF gene is missing. In Mycobacterium, the function of the trpF gene is performed by a dual-substrate (βα)8 phosphoribosyl isomerase (priA gene) also involved in L-histidine (hisA gene) biosynthesis. We investigated the effect of a HGT-acquired TrpF enzyme upon PriA’s substrate specificity in Corynebacterium through comparative genomics and phylogenetic reconstructions. After comprehensive in vivo and enzyme kinetic analyses of selected PriA homologs, a novel (βα)8 isomerase subfamily with a specialized function in L-histidine biosynthesis, termed subHisA, was confirmed. X-ray crystallography was used to reveal active-site mutations in subHisA important for narrowing of substrate specificity, which when mutated to the naturally occurring amino acid in PriA led to gain of function. Moreover, in silico molecular dynamic analyses demonstrated that the narrowing of substrate specificity of subHisA is concomitant with loss of ancestral protein conformational states. Our results show the importance of HGT in shaping enzyme evolution and metabolism.
Item Type: | Journal Article | ||||||||
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Subjects: | Q Science > QH Natural history > QH426 Genetics Q Science > QR Microbiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||
Library of Congress Subject Headings (LCSH): | Enzymes, Molecular genetics, Amino acids -- Metabolism , Genetics -- Research | ||||||||
Journal or Publication Title: | Molecular Biology and Evolution | ||||||||
Publisher: | Oxford University Press | ||||||||
ISSN: | 0737-4038 | ||||||||
Official Date: | 9 September 2013 | ||||||||
Dates: |
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Volume: | Volume 30 | ||||||||
Number: | Number 9 | ||||||||
Page Range: | pp. 2024-2034 | ||||||||
DOI: | 10.1093/molbev/mst115 | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Access rights to Published version: | Restricted or Subscription Access | ||||||||
Date of first compliant deposit: | 25 December 2015 | ||||||||
Date of first compliant Open Access: | 25 December 2015 | ||||||||
Funder: | Consejo Nacional de Ciencia y Tecnología (Mexico) [Mexican Council for Science and Technology] (CONACYT), Royal Society (Great Britain), Birmingham Science City | ||||||||
Grant number: | 50952-Q, 83039, 132376 (CONACYT) |
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