MOLECULAR-CLONING OF PLANT TRANSCRIPTS ENCODING PROTEIN-KINASE HOMOLOGS
MOLECULAR-CLONING OF PLANT TRANSCRIPTS ENCODING PROTEIN-KINASE HOMOLOGS
复制标题
DOI：
10.1073/pnas.86.9.3140
复制
发表时间：
1989-05-01
影响因子：
11.1
通讯作者：
LAMB, CJ
中科院分区：
文献类型：
--
作者：
LAWTON, MA;YAMAMOTO, RT;LAMB, CJ
Oligonucleotides, corresponding to conserved regions of animal protein-serine/threonine kinases, were used to isolate cDNAs encoding plant homologs in the dicot bean (Phaseolus vulgaris L.) and the monocot rice (Oryza sativa L.). The C-terminal regions of the deduced polypeptides encoded by the bean (PVPK-1) and rice (G11A) cDNAs, prepared from mRNAs of suspension cultures and leaves, respectively, contain features characteristic of the catalytic domains of eukaryotic protein-serine/thereonine kinases, indicating that these cDNAs encode plant protein kinases. The putative catalytic domains are most closely related to cyclic nucleotide-dependent protein kinases and the protein kinase C family, suggesting the plant homologs may likewise transduce extracellular signals. However, outside these domains, PVPK-1 and G11A exhibit no homology either to each other or to regulatory domains of other protein kinases, indicating the plant homologs are modulated by other signals. PVPK-1 corresponds to a 2.4-kb transcript in suspension cultured bean cells. Southern blots of genomic DNA indicate that PVPK-1 and G11A correspond to single copy genes that form part of a family of related plant sequences.
