Molecular cloning and expression of a MAP kinase homologue from pea

Stafstrom, Joel P.; Altschuler, Mitchell; Anderson, David H.

doi:10.1007/bf00038997

Cited by 87 publications

(56 citation statements)

References 40 publications

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“…ATMPK6 shows high homology to MsERKl (88.4%) and PsMAP (87.1%) not only in the catalytic domains but also in both the N-and C-terminal regions and in the divergent regions between subdomains VII and VIII [14]. This suggests that ATMPK6 is a counterpart of MsERKl [16] and PsMAP [17]. An S. pombe MAP kinase, Spkl, is essential for mating.…”

Section: Discussionmentioning

confidence: 99%

ATMPKs: a gene family of plant MAP kinases in Arabidopsis thaliana

Mizoguchi¹,

Hayashida²,

Yamaguchi-Shinozaki³

et al. 1993

FEBS Letters

137

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We previously reported two cDNAs for MAP kinases (cATMPK1 and cATMPK2) from a dicot plant, Arabidopsis thaliana. We describe here the cloning and characterization of five additional cDNAs encoding novel MAP kinases in Arabidopsis, cATMPK3, cATMPK4, cATMPK5, cATMPK6, and cATMPK7. The amino acid residues corresponding to the sites of phosphorylation (Thr-Glu-Tyr) that are involved in the activation of animal MAP kinases are conserved in all the seven putative ATMPK proteins. Genes for MAP kinases in Arabidopsis constitute a family that contains more than seven members. Sequence analysis suggests that there are at least three subfamilies in the family of Arabidopsis genes for MAP kinases.

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Section: Discussionmentioning

confidence: 99%

ATMPKs: a gene family of plant MAP kinases in Arabidopsis thaliana

Mizoguchi¹,

Hayashida²,

Yamaguchi-Shinozaki³

et al. 1993

FEBS Letters

137

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“…These results strongly suggest that OsMEK1 is a partner of Os-MAP1 in rice. (Takezawa, 1999), PsMAPK from pea (Pisum sativum; Stafstrom et al, 1993), SIPK (Zhang and Klessig, 1997) and WIPK (Seo et al, 1995) from tobacco, ZmMPK from maize (Berberich et al, 1999), AtMPK3 from Arabidopsis (Mizoguchi et al, 1993), and MMK4 from alfalfa (Jonak et al, 1996). Sequences are aligned, and gaps (dashes) have been introduced to maximize the alignment.…”

Section: Osmek1 Interacts With Osmap1 But Not With Osmap2 and Osmap3 mentioning

confidence: 99%

Two Novel Mitogen-Activated Protein Signaling Components, OsMEK1 and OsMAP1, Are Involved in a Moderate Low-Temperature Signaling Pathway in Rice

2002

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Rice (Oryza sativa) anther development is easily damaged by moderately low temperatures above 12°C. Subtractive screening of cDNA that accumulated in 12°C-treated anthers identified a cDNA clone, OsMEK1, encoding a protein with features characteristic of a mitogen-activated protein (MAP) kinase kinase. The putative OsMEK1 protein shows 92% identity to the maize (Zea mays) MEK homolog, ZmMEK1. OsMEK1 transcript levels were induced in rice anthers by 12°C treatment for 48 h. Similar OsMEK1 induction was observed in shoots and roots of seedlings that were treated at 12°C for up to 24 h. It is interesting that no induction of OsMEK1 transcripts was observed in 4°C-treated seedlings. In contrast, rice lip19, encoding a bZIP protein possibly involved in low temperature signal transduction, was not induced by 12°C treatment but was induced by 4°C treatment. Among the three MAP kinase homologs cloned, only OsMAP1 displayed similar 12°C-specific induction pattern as OsMEK1. A yeast two-hybrid system revealed that OsMEK1 interacts with OsMAP1, but not with OsMAP2 and OsMAP3, suggesting that OsMEK1 and OsMAP1 probably function in the same signaling pathway. An in-gel assay of protein kinase activity revealed that a protein kinase (approximately 43 kD), which preferentially uses myelin basic protein as a substrate, was activated by 12°C treatment but not by 4°C treatment. Taken together, these results lead us to conclude that at least two signaling pathways for low temperature stress exist in rice, and that a MAP kinase pathway with OsMEK1 and OsMAP1 components is possibly involved in the signaling for the higher range low-temperature stress.Rice (Oryza sativa) is widely cultivated in a large number of different natural environments (Nishiyama, 1984). Compared with other cereal crops such as wheat (Triticum aestivum) and barley (Hordeum vulgare), rice is much more sensitive to low temperature as a result of its tropical origin. Male sterility is the most severe consequence among the many chilling-induced agronomic damages in rice production. The developmental stages from pollen formation to fertilization are the most vulnerable to low temperature throughout the life cycle of rice plants (Nishiyama, 1984). It has been reported that the young microspore stage in pollen development was the most sensitive to low temperature (Satake and Hayase, 1970). Exposure of rice plants at the tetrad stage to a moderately low temperature (12°C) for 4 d resulted in male sterility in 80% of spikelets (Satake and Hayase, 1970; Nishiyama, 1984). Microscopic observation of developing rice anthers suggested that one possible reason for the male sterility after lowtemperature treatment was the failure of anther development. The observed abnormalities included the cessation of anther development, the arrest of pollen development, anthers remaining within the flowers after anthesis, and partial or no dehiscence (Satake, 1976). Cytological observation revealed a dilatation of tapetal layers in chilling-treated rice anthers (Nishiyama, 1976(Nishiyama,...

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“…Moreover, the characteristics of the elicitor activated kinase resemble those of MAPK. The existence of the MAP kinase/ extracellular signal-regulated protein kinase family has already been demonstrated in several plant species [39][40][41][42][43]. It may also be possible that tyrosine-phosphorylated residues within the phytochrome molecule serve as binding sites for proteins containing SH2 (src homology) domains.…”

Section: !:I !ĩ!:I I !I I !I I I I I ĩ I I ĩI I I ! I I ! ! I J !I I mentioning

confidence: 99%

A possible tyrosine phosphorylation of phytochrome

1996

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Red/far-red light signal transduetion by the phytochrome family of photoreceptors regulates plant growth and development. We investigated the possibility that tyrosine kinases and/or phosphatases are involved in phytochromemediated signal transduction using crude extracts of oat seedlings that are grown in the dark. We found that a 124 kDa protein was tyrosine-phosphorylated as determined by Western blotting with a phosphotyrosine-specific monoclonal antibody. The 124 kDa protein was recognized by the anti-phosphotyrosine antibody in anti-phytochrome A immunoprecipitates. The level of anti-phosphotyrosinc antibody binding to the 124 kDa protein(s) in phytochrome immunoprecipitates that had been treated with red light prior to immunoprecipitation decreased relative to dark controls. These results suggest that either phytochrome from dark-grown seedlings is tyrosine phosphorylated or that it coimmunoprecipitates with a phosphotyrosine-containing protein of the same molecular weight. The implications of these results in the regulation of (a) the putative Ser/Thr kinase activity of the photoreceptor and (b) the binding of signaling molecules, such as phospholipase C to phytochrome, are discussed.

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Molecular cloning and expression of a MAP kinase homologue from pea

Cited by 87 publications

References 40 publications

ATMPKs: a gene family of plant MAP kinases in Arabidopsis thaliana

ATMPKs: a gene family of plant MAP kinases in Arabidopsis thaliana

Two Novel Mitogen-Activated Protein Signaling Components, OsMEK1 and OsMAP1, Are Involved in a Moderate Low-Temperature Signaling Pathway in Rice

A possible tyrosine phosphorylation of phytochrome

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