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dc.contributor.author
Asención Diez, Matías Damián
dc.contributor.author
Miah, Farzana
dc.contributor.author
Stevenson, Clare E. M.
dc.contributor.author
Lawson, David M.
dc.contributor.author
Iglesias, Alberto Alvaro
dc.contributor.author
Bornemann, Stephen
dc.date.available
2018-05-18T20:57:54Z
dc.date.issued
2017-01
dc.identifier.citation
Asención Diez, Matías Damián; Miah, Farzana; Stevenson, Clare E. M.; Lawson, David M.; Iglesias, Alberto Alvaro; et al.; The production and utilization of GDP-glucose in the biosynthesis of trehalose-6-phosphate by Streptomyces venezuelae; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 292; 1-2017; 945-954
dc.identifier.issn
0021-9258
dc.identifier.uri
http://hdl.handle.net/11336/45674
dc.description.abstract
Trehalose-6-phosphate synthase OtsA from streptomycetes is unusual in that it uses GDP-glucose as the donor substrate rather than the more commonly used UDP-glucose. We now confirm that OtsA from Streptomyces venezuelae has such a preference for GDP-glucose and can utilize ADP-glucose to some extent too. A crystal structure of the enzyme shows that it shares twin Rossmann-like domains with the UDP-glucose-specific OtsA from Escherichia coli. However, it is structurally more similar to Streptomyces hygroscopicus VldE, a GDP-valienol-dependent pseudoglycosyltransferase enzyme. Comparison of the donor binding sites reveals that the amino acids associated with the binding of diphosphoribose are almost all identical in these three enzymes. By contrast, the amino acids associated with binding guanine in VldE (Asn, Thr, and Val) are similar in S. venezuelae OtsA (Asp, Ser, and Phe, respectively) but not conserved in E. coli OtsA (His, Leu, and Asp, respectively), providing a rationale for the purine base specificity of S. venezuelae OtsA. To establish which donor is used in vivo, we generated an otsA null mutant in S. venezuelae. The mutant had a cell density-dependent growth phenotype and accumulated galactose 1-phosphate, glucose 1-phosphate, and GDP-glucose when grown on galactose. To determine how the GDP-glucose is generated, we characterized three candidate GDP-glucose pyrophosphorylases. SVEN_3027 is a UDP-glucose pyrophosphorylase, SVEN_3972 is an unusual ITP-mannose pyrophosphorylase, and SVEN_2781 is a pyrophosphorylase that is capable of generating GDP-glucose as well as GDP-mannose. We have therefore established how S. venezuelae can make and utilize GDP-glucose in the biosynthesis of trehalose 6-phosphate.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Biochemistry and Molecular Biology
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Trehalose-6p
dc.subject
Actinobacteria
dc.subject
Glucosyltransferase
dc.subject
Gdp-Glucose
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
The production and utilization of GDP-glucose in the biosynthesis of trehalose-6-phosphate by Streptomyces venezuelae
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-05-11T21:16:58Z
dc.journal.volume
292
dc.journal.pagination
945-954
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Asención Diez, Matías Damián. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
dc.description.fil
Fil: Miah, Farzana. John Innes Institute; Reino Unido
dc.description.fil
Fil: Stevenson, Clare E. M.. John Innes Institute; Reino Unido
dc.description.fil
Fil: Lawson, David M.. John Innes Institute; Reino Unido
dc.description.fil
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
dc.description.fil
Fil: Bornemann, Stephen. John Innes Institute; Reino Unido
dc.journal.title
Journal of Biological Chemistry (online)
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/292/3/945
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M116.758664


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