Autor: |
Sang Dai Park, Yong Hwan Jin, Rho Hyun Seong, Seung Hae Kim, Chee‐Gun Lee, Seung Hwan Hong, Yeun Kyu Jang, Eung Jae Yoo |
Rok vydání: |
1998 |
Předmět: |
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Zdroj: |
Korean Journal of Biological Sciences. 2:539-543 |
ISSN: |
1226-5071 |
DOI: |
10.1080/12265071.1998.9647457 |
Popis: |
Hrp1, of Schizosaccharomyces pombe, is a new member of the SWI2/SNF2 protein family that contains a chromodomain and a DNA binding domain as well as ATPase/7 helicase domains. This configuration suggests that Hrp1 could be a homolog of mouse CHD1, which is thought to function in altering the chromatin structure to facilitate gene expression. To understand the enzymatic nature of Hrp1, we purified the 6‐Histidine‐tagged Hrp1 protein (6×His‐Hrp1) to homogeneity from a S. pombe Hrp1‐overexpressing strain and then examined its biochemical properties. We demonstrate that the purified 6×His‐Hrp1 protein exhibited a DNA‐binding activity with a moderate preference to the (A+T)‐rich tract in double‐stranded DNA via a minor groove interaction. However, we failed to detect any intrinsic DNA helicase activity from the purified Hrp1 like other SWI2/SNF2 proteins. These observations suggest that the DNA binding activities of Hrp1 may be involved in the remodeling of the chromatin structure with DNA‐dependent ATPase. We... |
Databáze: |
OpenAIRE |
Externí odkaz: |
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