These authors contributed equally to this work.
Original Article
OsCYP2, a chaperone involved in degradation of auxin-responsive proteins, plays crucial roles in rice lateral root initiation
Article first published online: 4 MAR 2013
DOI: 10.1111/tpj.12106
© 2013 The Authors The Plant Journal © 2013 Blackwell Publishing Ltd
Additional Information
How to Cite
Kang, B., Zhang, Z., Wang, L., Zheng, L., Mao, W., Li, M., Wu, Y., Wu, P. and Mo, X. (2013), OsCYP2, a chaperone involved in degradation of auxin-responsive proteins, plays crucial roles in rice lateral root initiation. The Plant Journal, 74: 86–97. doi: 10.1111/tpj.12106
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These authors contributed equally to this work.
Publication History
- Issue published online: 19 MAR 2013
- Article first published online: 4 MAR 2013
- Accepted manuscript online: 5 JAN 2013 11:35AM EST
- Manuscript Accepted: 20 DEC 2012
- Manuscript Revised: 18 DEC 2012
- Manuscript Received: 3 AUG 2012
Funded by
- National High Technology Research and Development Program of China 863. Grant Number: 2007AA10Z118
- National Basic Research and Development Program of China. Grant Number: 2011CB100300
- Fundamental Research Funds for the Central Universities
Keywords:
- cyclophilin;
- lateral root initiation;
- auxin;
- protein interaction;
- Oryza sativa
Summary
Auxin plays a pivotal role in many facets of plant development. It acts by inducing the interaction between auxin-responsive [auxin (AUX)/indole-3-acetic acid (IAA)] proteins and the ubiquitin protein ligase SCFTIR to promote the degradation of the AUX/IAA proteins. Other cofactors and chaperones that participate in auxin signaling remain to be identified. Here, we characterized rice (Oryza sativa) plants with mutations in a cyclophilin gene (OsCYP2). cyp2 mutants showed defects in auxin responses and exhibited a variety of auxin-related growth defects in the root. In cyp2 mutants, lateral root initiation was blocked after nuclear migration but before the first anticlinal division of the pericycle cell. Yeast two-hybrid and in vitro pull-down results revealed an association between OsCYP2 and the co-chaperone Suppressor of G2 allele of skp1 (OsSGT1). Luciferase complementation imaging assays further supported this interaction. Similar to previous findings in an Arabidopsis thaliana SGT1 mutant (atsgt1b), degradation of AUX/IAA proteins was retarded in cyp2 mutants treated with exogenous 1-naphthylacetic acid. Our results suggest that OsCYP2 participates in auxin signal transduction by interacting with OsSGT1.

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