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Binding of an arm repeat protein to the kinase domain of the S-locus receptor kinase.

ABSTRACT: Screening of a yeast two-hybrid library for proteins that interact with the kinase domain of an S-locus receptor kinase (SRK) resulted in the isolation of a plant protein called ARC1 (Arm Repeat Containing). This interaction was mediated by the C-terminal region of ARC1 in which five arm repeat units were identified. Using the yeast two-hybrid system and in vitro binding assays, ARC1 was found to interact specifically with the kinase domains from SRK-910 and SRK-A14 but failed to interact with kinase domains from two different Arabidopsis receptor-like kinases. In addition, treatment with a protein phosphatase or the use of a kinase-inactive mutant reduced or abolished the binding of ARC1 to the SRK-910 kinase domain, indicating that the interaction was phosphorylation dependent. Lastly, RNA blot analysis revealed that the expression of ARC1 is restricted to the stigma, the site of the self-incompatibility response.

SUBMITTER: Gu T

PROVIDER: S-EPMC18231 | biostudies-literature | 1998 Jan

REPOSITORIES: biostudies-literature

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Binding of an arm repeat protein to the kinase domain of the S-locus receptor kinase.

Gu T T Mazzurco M M Sulaman W W Matias D D DD Goring D R DR

Proceedings of the National Academy of Sciences of the United States of America 19980101 1

Screening of a yeast two-hybrid library for proteins that interact with the kinase domain of an S-locus receptor kinase (SRK) resulted in the isolation of a plant protein called ARC1 (Arm Repeat Containing). This interaction was mediated by the C-terminal region of ARC1 in which five arm repeat units were identified. Using the yeast two-hybrid system and in vitro binding assays, ARC1 was found to interact specifically with the kinase domains from SRK-910 and SRK-A14 but failed to interact with k ...[more]

PMID: 9419384

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