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Oligomeric Structures Determine the Biochemical Characteristics of Human Nucleoside Diphosphate Kinases

Title
Oligomeric Structures Determine the Biochemical Characteristics of Human Nucleoside Diphosphate Kinases
Authors
Kim S.Y.Song E.J.Chang K.H.Kim E.Chae S.-K.Lee H.Lee K.-J.
Ewha Authors
이공주
SCOPUS Author ID
이공주scopus
Issue Date
2001
Journal Title
Journal of Biochemistry and Molecular Biology
ISSN
1225-8687JCR Link
Citation
vol. 34, no. 4, pp. 355 - 364
Indexed
SCOPUS WOS scopus
Abstract
Major human Nucleoside diphosphate kinases (NDPKs) exist as hetero-oligomers, consisting of NDPK-A and NDPK-B, rather than homo-oligomer. To investigate their biological function depending on the oligomeric structure in vivo, we characterized the biochemical properties of cellular NDPK. Cellular NDPKs, which are made up of a unique combination of isoforms, were purified from human erythrocyte and placenta. We found that cellular NDPK and recombinant isoforms NDPKs have their own distinct biochemical properties in autophosphorylation, stability toward heat or urea, and DNA binding. Cellular NDPK was found to have unique characteristics rather than the expected additive properties of recombinant isoforms. The mutations in the dimeric interface of NDPK-B (R34G, N69H or K135L) caused defective DNA binding and simultaneously reduced the enzymatic stability. These results suggest that the oligomeric interaction could play a major role in the stability of catalytic domain and might be related to the regulation of various cellular functions of NDPK.
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약학대학 > 약학과 > Journal papers
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