Document Detail


PLEIOTROPIC REGULATORY LOCUS 2 exhibits unequal genetic redundancy with its homolog PRL1.
MedLine Citation:
PMID:  22813545     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
In plants, signalling leading to resistance against biotrophic pathogens is complex. Perception of pathogenic microbes by resistance (R) proteins is relayed though successive activities of downstream components, in a network that is not well understood. PLEIOTROPIC REGULATORY LOCUS 1 (PRL1) and more than twenty other proteins are members of the MOS4-associated complex (MAC), a regulatory node in defence signalling. Of all characterized MAC members, mutations in PRL1 cause the most severe susceptibility towards both virulent and avirulent microbial pathogens. Genetic suppressors of prl1 represent new signalling elements and may aid in further unravelling of defence mechanisms. Our identification and characterization of a dominant suppressor of prl1 revealed a regulatory, gain-of-function mutation in PLEIOTROPIC REGULATORY LOCUS 2 (PRL2), a close homolog of PRL1. Loss-of-function mutants of PRL2 do not exhibit altered phenotypes, however prl1 prl2 double mutants exhibit enhanced morphological defects consistent with unequal genetic redundancy between the homologs. Up-regulated gene expression mediated by the dominant prl2-1D allele completely suppresses disease susceptibility in the prl1 mutant background and also restores wild-type appearance, further supporting functional equivalence between the two PRL proteins.
Authors:
Tabea Weihmann; Kristoffer Palma; Yukino Nitta; Xin Li
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-7-18
Journal Detail:
Title:  Plant & cell physiology     Volume:  -     ISSN:  1471-9053     ISO Abbreviation:  -     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-7-20     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9430925     Medline TA:  Plant Cell Physiol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Michael Smith Laboratories, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.
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