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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2018.1
- 수록면
- 315 - 321 (7page)
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Molecular and functional characterization of proteins and their levels is of great interest in understanding the mechanism of diverse cellular processes. In this study, we report on the convenient Escherichia coli-based protein expression system that allows recombinant of soluble proteins expression and cytosolic domain of membrane-localised kinases, followed by the detection of autophosphorylation activity in protein kinases. This approach is applied to regulatory proteins of Arabidopsis thaliana, including 14-3-3, calmodulin, calcium-dependent protein kinase, TERMINAL FLOWER 1(TFL1), FLOWERING LOCUS T (FT), receptorlike cytoplasmic kinase and cytoplasmic domain of leucine-rich repeat-receptor like kinase proteins. Our Western blot analysis which uses phospho-specific antibodies showed that five putative LRR-RLKs and two putative RLCKs have autophosphorylation activity in vitro on threonine and/or tyrosine residue(s), suggesting their potential role in signal transduction pathways. Our findings were also discussed in the broader context of recombinant expression and biochemical analysis of soluble and membrane-localised receptor kinases in microbial systems.
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참고문헌 (47)
참고문헌 신청
Antoln-Llovera M / 2012 / Receptor kinase signaling pathways in plant-microbe interactions / Annu. Rev. Phytopathol 50:451~473
Babu YS / 1988 / Structure of calmodulin refined at 2.2 Å resolution / Journal of molecular biology 204:191~204
Becraft PW / 2002 / Receptor kinase signaling in plant development / Annu. Rev. Cell Dev. Biol 18:163~192
Bentem SF / 2009 / Protein tyrosine phosphorylation in plants: more abundant than expected? / Trends in Plant Science 14:71~76
채원병 / 2016 / Plant receptor kinases bind and phosphorylate 14-3-3 proteins / Genes & Genomics 38(11):1111~1119
Babu YS / 1988 / Structure of calmodulin refined at 2.2 Å resolution / Journal of molecular biology 204:191~204
Becraft PW / 2002 / Receptor kinase signaling in plant development / Annu. Rev. Cell Dev. Biol 18:163~192
Bentem SF / 2009 / Protein tyrosine phosphorylation in plants: more abundant than expected? / Trends in Plant Science 14:71~76
채원병 / 2016 / Plant receptor kinases bind and phosphorylate 14-3-3 proteins / Genes & Genomics 38(11):1111~1119
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