Document Detail


Structural and functional characterization of the protein kinase Mps1 in Arabidopsis thaliana.
MedLine Citation:
PMID:  23049844     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In eukaryotes, protein kinases catalyze the transfer of a gamma-phosphate from ATP (or GTP) to specific amino acids in protein targets. In plants, protein kinases have been shown to participate in signaling cascades driving responses to environmental stimuli and developmental processes. Plant meristems are undifferentiated tissues that provide the major source of cells that will form organs throughout development. However, non-dividing specialized cells can also dedifferentiate and re-initiate cell division if exposed to appropriate conditions. Mps1 (Monopolar spindle) is a dual-specificity protein kinase that plays a critical role in monitoring the accuracy of chromosome segregation in the mitotic checkpoint mechanism. Although Mps1 functions have been clearly demonstrated in animals and fungi, its role in plants is so far unclear. Here, using structural and biochemical analyses here we show that Mps1 has highly similar homologs in many plant genomes across distinct lineages (e.g. AtMps1 in Arabidopsis thaliana). Several structural features (i.e. catalytic site, DFG motif and threonine triad) are clearly conserved in plant Mps1 kinases. Structural and sequence analysis also suggest that AtMps1 interact with other cell cycle proteins, such as Mad2 and MAPK1. By using a very specific Mps1 inhibitor (SP600125) we show that compromised AtMps1 activity hampers the development of A. thaliana seedlings in a dose-dependent manner, especially in secondary roots. Moreover, concomitant administration of the auxin IAA neutralizes the AtMps1 inhibition phenotype, allowing secondary root development. These observations let us to hypothesize that AtMps1 might be a downstream regulator of IAA signaling in the formation of secondary roots. Our results indicate that Mps1 might be a universal component of the Spindle Assembly Checkpoint machinery across very distant lineages of eukaryotes.
Authors:
Eduardo Alves Gamosa de Oliveira; Nelilma Correia Romeiro; Elane da Silva Ribeiro; Claudete Santa-Catarina; Antônia Elenir Amâncio Oliveira; Vanildo Silveira; Gonçalo Apolinário de Souza Filho; Thiago Motta Venancio; Marco Antônio Lopes Cruz
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-09-26
Journal Detail:
Title:  PloS one     Volume:  7     ISSN:  1932-6203     ISO Abbreviation:  PLoS ONE     Publication Date:  2012  
Date Detail:
Created Date:  2012-10-10     Completed Date:  2013-05-07     Revised Date:  2013-07-11    
Medline Journal Info:
Nlm Unique ID:  101285081     Medline TA:  PLoS One     Country:  United States    
Other Details:
Languages:  eng     Pagination:  e45707     Citation Subset:  IM    
Affiliation:
Laboratório de Biotecnologia Vegetal, Núcleo em Ecologia e Desenvolvimento Sócio-ambiental de Macaé, Universidade Federal do Rio de Janeiro, Macaé, Rio de Janeiro, Brazil.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Motifs
Amino Acid Sequence
Arabidopsis / metabolism*
Arabidopsis Proteins / chemistry*
Catalysis
Cell Cycle Proteins / chemistry*
Enzyme Inhibitors / pharmacology
Evolution, Molecular
Gene Expression Regulation, Plant*
Genome, Plant
Molecular Conformation
Molecular Sequence Data
Phosphorylation
Phylogeny
Plant Roots / metabolism
Protein Kinases / chemistry*
Protein-Serine-Threonine Kinases / chemistry*
Protein-Tyrosine Kinases / chemistry*
Sequence Homology, Amino Acid
Signal Transduction
Chemical
Reg. No./Substance:
0/Arabidopsis Proteins; 0/Cell Cycle Proteins; 0/Enzyme Inhibitors; EC 2.7.-/Mps1 protein, Arabidopsis; EC 2.7.-/Protein Kinases; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.12.1/TTK protein, human
Comments/Corrections

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