Identification of physiological substrate for a newly identified serine/threonine/tyrosine protein kinase from Arabidopsis thaliana

Ram Rajasekharan, . and Ho Hooi Ling, . (2011) Identification of physiological substrate for a newly identified serine/threonine/tyrosine protein kinase from Arabidopsis thaliana. [Proceedings Paper]

Protein phosphorylation plays prominent role in various biochemical pathways in plant as a result of active implication in the regulation of cell growth and development. Our previous laboratory studies revealed erine hreonine and yrosine protein kinases STYK from peanut possessed essential role in the regulation of dual specificity kinase activity. The analysis of STYK from Genevestigator revealed protein expression of STYK occurred during seed germination silique formation and senescent leaves development. However in vivo physiological substrate for the protein kinase is yet to be identified to uncover its physiological role in Arabidopsis. Therefore the objectives of study are to identify in vivo substrate for a newly isolated erine hreonine yrosine protein kinase from Arabidopsis thaliana AtSTYK and thereafter to reveal its physiological role in plant system. What is the physiological substrate for AtSTYK to transfer a phosphate group To address this protein-protein Interaction via yeast two-hybrid system was used to detect positive interactors of AtSTYK. The results showed that OBERON1 OBE1 with its paralog OBERON2 OBE2 genes were detected as the most frequent interacting partners for AtSTYK. Both OBERON genes encode for plant homeodomain PHD finger proteins were phosphorylated by AtSTYK. This result indicates AtSTYK plays a putative role in the maintenance and establishment of apical meristems as well as preservation of stem cells population within the apical meristems region.

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Abstract

Protein phosphorylation plays prominent role in various biochemical pathways in plant as a result of active implication in the regulation of cell growth and development. Our previous laboratory studies revealed erine hreonine and yrosine protein kinases STYK from peanut possessed essential role in the regulation of dual specificity kinase activity. The analysis of STYK from Genevestigator revealed protein expression of STYK occurred during seed germination silique formation and senescent leaves development. However in vivo physiological substrate for the protein kinase is yet to be identified to uncover its physiological role in Arabidopsis. Therefore the objectives of study are to identify in vivo substrate for a newly isolated erine hreonine yrosine protein kinase from Arabidopsis thaliana AtSTYK and thereafter to reveal its physiological role in plant system. What is the physiological substrate for AtSTYK to transfer a phosphate group To address this protein-protein Interaction via yeast two-hybrid system was used to detect positive interactors of AtSTYK. The results showed that OBERON1 OBE1 with its paralog OBERON2 OBE2 genes were detected as the most frequent interacting partners for AtSTYK. Both OBERON genes encode for plant homeodomain PHD finger proteins were phosphorylated by AtSTYK. This result indicates AtSTYK plays a putative role in the maintenance and establishment of apical meristems as well as preservation of stem cells population within the apical meristems region.

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Item Type:	Proceedings Paper
Additional Information:	Available at Perpustakaan Sultan Abdul Samad Universiti Putra Malaysia 43400 UPM Serdang Selangor Malaysia. QR22 M3I61 2011 vol.2 Call Number.
AGROVOC Term:	Arabidopsis thaliana
AGROVOC Term:	Serine
AGROVOC Term:	Threonine
AGROVOC Term:	Tyrosine
AGROVOC Term:	Cloning
AGROVOC Term:	Centrifuging
AGROVOC Term:	Enzymes
AGROVOC Term:	Nucleotide sequence
AGROVOC Term:	Genes
AGROVOC Term:	Proteolysis
Geographical Term:	MALAYSIA
Depositing User:	Ms. Suzila Mohamad Kasim
Last Modified:	24 Apr 2025 05:15
URI:	http://webagris.upm.edu.my/id/eprint/12974

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