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標題: OIP30, a RuvB-Like DNA Helicase 2, is a Potential Substrate for the Pollen-Predominant OsCPK25/26 in Rice
作者: Wang, C.W.
Chen, W.C.
Lin, L.J.
Lee, C.T.
Tseng, T.H.
Leu, W.M.
關鍵字: Calcium-dependent protein kinase;Oryza sativa L;Pollen;RuvB-like DNA;Helicase;Substrate;dependent protein-kinase;gene-expression;mesembryanthemum-crystallinum;sucrose synthase;seed development;oryza-sativa;tube growth;in-vitro;calcium;phosphorylation
Project: Plant and Cell Physiology
期刊/報告no:: Plant and Cell Physiology, Volume 52, Issue 9, Page(s) 1641-1656.
Calcium ions are a well-known essential component for pollen germination and tube elongation. Several calcium-dependent protein kinases (CDPKs) are expressed predominantly in mature pollen grains and play a critical role in pollen. However, none of their interacting proteins or downstream substrates has been identified. Using yeast two-hybrid screening, we isolated OsCPK25/26-interacting protein 30 (OIP30), which is also predominantly expressed in pollen. OIP30 encodes a RuvB-like DNA helicase 2 (RuvBL2) that is well conserved in eukaryotic species from yeast to human. Yeast and Drosophila defective in RuvBL2 are non-viable. The interaction between OsCPK26 and OIP30 was confirmed by far-Western blot and pull-down experiments. OIP30 was phosphorylated in a calcium-dependent manner by OsCPK26 but not OsCPK2, which is highly similar to OsCPK26 in sequence and expression profile. OIP30 unwound partial duplex DNA with a 3' to 5' directionality by ATP hydrolysis. Concurrently, the ATPase activity of OIP30 depended on single-stranded DNA. OsCPK26 phosphorylated OIP30 and enhanced both its helicase and ATPase activity about 3-fold. OIP30 may be the potential downstream substrate for OsCPK25/26 in pollen. This report characterizes a RuvBL in plants and links its activities with its upstream regulator.
ISSN: 0032-0781
DOI: 10.1093/pcp/pcr094
Appears in Collections:生物科技學研究所

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