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Cytokinin affinity purification and identification of a tobacco BY‐2 adenosine kinase
Author(s) -
Laukens Kris,
Lenobel René,
Strnad Miroslav,
Van Onckelen Harry,
Witters Erwin
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03750-x
Subject(s) - cytokinin , adenosine kinase , identification (biology) , adenosine , biochemistry , chemistry , kinase , computational biology , biology , botany , gene , adenosine deaminase , auxin
Adenosine kinase is one of the enzymes potentially responsible for the formation of cytokinin nucleotides in plants. Using a zeatin affinity column a 40 kDa protein was isolated from tobacco Bright Yellow 2 (TBY‐2) and identified by mass spectrometry as adenosine kinase. The ligand interaction reported here can be disrupted by several other adenine‐ but not guanine‐based purine derivatives. The observed interaction with cytokinins is discussed in view of a putative role for adenosine kinase in TBY‐2 cytokinin metabolism. The presented results show for the first time a plant adenosine kinase affinity‐purified to homogeneity that was identified by primary structure analysis.