Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractStructure-activity relationship of gelatinase biosynthesis-activating pheromone of Enterococcus faecalis    Next AbstractS-like ribonuclease gene expression in carnivorous plants »

Plant J


Title:Possible involvement of differential splicing in regulation of the activity of Arabidopsis ANP1 that is related to mitogen-activated protein kinase kinase kinases (MAPKKKs)
Author(s):Nishihama R; Banno H; Kawahara E; Irie K; Machida Y;
Address:"Division of Biological Science, Graduate School of Science, Nagoya University, Japan"
Journal Title:Plant J
Year:1997
Volume:12
Issue:1
Page Number:39 - 48
DOI: 10.1046/j.1365-313x.1997.12010039.x
ISSN/ISBN:0960-7412 (Print) 0960-7412 (Linking)
Abstract:"Three types of Arabidopsis cDNA (cANP1, cANP2 and cANP3) have been isolated that encode putative protein kinases, designated ANP1, ANP2 and ANP3. These kinases exhibit a high degree of homology to NPK1, a tobacco protein that is a member of the family of mitogen-activated protein kinase kinase kinases (MAPKKKs), which appears to function in the proliferation of tobacco cells. The predicted amino acid sequences of the kinase domains in the amino-terminal halves of the ANPs were more than 80% identical to that of NPK1, while the kinase-unrelated regions in the carboxy-terminal halves exhibited relatively low homology. Two species of cANP1 were identified, ANP1L cDNA (cANP1L) and ANP1S cDNA (cANP1S), which were derived from a single ANP1 gene: the former had an intron-like sequence in the coding region for the kinase-unrelated region, while the latter did not include such an intron-like sequence. cANP1L encoded a putative protein with both kinase and kinase-unrelated domains, resembling NPK1, whereas cANP1S encoded only the amino-terminal kinase domain because the intron-like sequence was absent, with resulting elimination of most of the kinase-unrelated region. Genetic analysis with mutant yeast cells showed that over-expression of cANP1L or of cANP1S activated the mating pheromone-responsive signal pathway which is mediated by a MAP kinase cascade. Moreover, the extent of such activation by cANP1S was greater than that by cANP1L. These results predict that differential splicing of the intron-like sequence in the ANP1 transcript might be at least one of the molecular mechanisms involved in the generation of active ANP1 protein kinase"
Keywords:"*Alternative Splicing Amino Acid Sequence Arabidopsis/*enzymology/genetics Arabidopsis Proteins/*metabolism Base Sequence Cloning, Molecular Gene Expression Regulation, Enzymologic *Gene Expression Regulation, Plant Genes, Plant MAP Kinase Kinase Kinases/;"
Notes:"MedlineNishihama, R Banno, H Kawahara, E Irie, K Machida, Y eng Comparative Study Research Support, Non-U.S. Gov't England 1997/07/01 Plant J. 1997 Jul; 12(1):39-48. doi: 10.1046/j.1365-313x.1997.12010039.x"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 27-12-2024