View : 13 Download: 0
Oligomeric Structures Determine the Biochemical Characteristics of Human Nucleoside Diphosphate Kinases
- Oligomeric Structures Determine the Biochemical Characteristics of Human Nucleoside Diphosphate Kinases
- Kim S.Y.; Song E.J.; Chang K.H.; Kim E.; Chae S.-K.; Lee H.; Lee K.-J.
- Ewha Authors
- SCOPUS Author ID
- Issue Date
- Journal Title
- Journal of Biochemistry and Molecular Biology
- vol. 34, no. 4, pp. 355 - 364
- 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.
- Appears in Collections:
- 약학대학 > 약학과 > Journal papers
- Files in This Item:
There are no files associated with this item.
- RIS (EndNote)
- XLS (Excel)
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.