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Functional characterization of the rice kaurene synthase-like gene family.

Functional characterization of the rice kaurene synthase-like gene family. Research Abstract Details 

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  • Functional characterization of the rice kaurene synthase-like gene family. Abstract Text:

    meimei xuMeimei Xu,p ross wildermanP Ross Wilderman,dana morroneDana Morrone,jianjun xuJianjun Xu,arnab royArnab Roy,marcia margis-pinheiroMarcia Margis-Pinheiro,narayana m upadhyayaNarayana M Upadhyaya,robert m coatesRobert M Coates,reuben j petersReuben J Peters,

    The rice (Oryza sativa) genome contains a family of kaurene synthase-like genes (OsKSL) presumably involved in diterpenoid biosynthesis. While a number of OsKSL enzymes have been functionally characterized, several have not been previously investigated, and the gene family has not been broadly analyzed. Here we report cloning of several OsKSL genes and functional characterization of the encoded enzymes. In particular, we have verified the expected production of ent-kaur-16-ene by the gibberellin phytohormone biosynthesis associated OsKS1 and demonstrated that OsKSL3 is a pseudo-gene, while OsKSL5 and OsKSL6 produce ent-(iso)kaur-15-ene. Similar to previous reports, we found that our sub-species variant of OsKSL7 produces ent-cassa-12,15-diene, OsKSL10 produces ent-(sandaraco)pimar-8(14),15-diene, and OsKSL8 largely syn-stemar-13-ene, although we also identified syn-stemod-12-ene as an alternative product formed in approximately 20% of the reactions catalyzed by OsKSL8. Along with our previous reports identifying OsKSL4 as a syn-pimara-7,15-diene synthase and OsKSL11 as a syn-stemod-13(17)-ene synthase, this essentially completes biochemical characterization of the OsKSL gene family, enabling broader analyses. For example, because several OsKSL enzymes are involved in phytoalexin biosynthesis and their gene transcription is inducible, promoter analysis was used to identify a pair of specifically conserved motifs that may be involved in transcriptional up-regulation during the rice plant defense response. Also examined is the continuing process of gene evolution in the OsKSL gene family, which is particularly interesting in the context of very recently reported data indicating that a japonica sub-species variant of OsKSL5 produces ent-pimara-8(14),15-diene, rather than the ent-(iso)kaur-15-ene produced by the indica sub-species variant analyzed here.

    Functional characterization of the rice kaurene synthase-like gene family. Publishing Authors By Initials

    m xuM Xu,pr wildermanPR Wilderman,d morroneD Morrone,j xuJ Xu,a royA Roy,m margis-pinheiroM Margis-Pinheiro,nm upadhyayaNM Upadhyaya,rm coatesRM Coates,rj petersRJ Peters,

    For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research

    PUBMED ID PMID:

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    Functional characterization of the rice kaurene synthase-like gene family. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: Phytochemistry

    VOLUME: 68

    Page Numbers: 312-26

    Journal Abbreviation: Phytochemistry

    ISSN: 0031-9422

    DAY: 1

    MONTH: 12

    YEAR: 2006

    Functional characterization of the rice kaurene synthase-like gene family. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 151434

    Functional characterization of the rice kaurene synthase-like gene family. Keywords Mesh Terms:

    KEYWORDS: Sequence Homology, Amino Acid

    MESH TERMS: enzymology

    Chemical & Substance for Abstract: Functional characterization of the rice kaurene synthase-like gene family. Information

    Substance Name: kaurene synthetase

    Registry Number: EC 2.5.1.-

    Grant and Affiliation Information for Functional characterization of the rice kaurene synthase-like gene family.

    AFFILIATION: Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, IA 50011, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIGMS

    GRANT: GM13956

    ACRONYM: GM

    MEDLINETA: Phytochemistry

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