The novel protein BC1 possesses ATPase activity
Date Issued
2005
Date
2005
Author(s)
Chang, Kung-Jen
DOI
en-US
Abstract
Previously our lab established the GCH dominant-negative (DN) cell lines. We found some cell lines do not present DN phenomenon. After analyzing the amount of RNA expression by Northen blot, we select a gene that was highly expressed in non dominant negative (non-DN) cell line. We named this gene BC1 (Brain coregulator 1).
BC1 is composed of 559 amino acid residues. Its molecular weight is about 70 kilodalton. In the C-terminus of BC1, we found a conserved region similar to YT521b protein, and it is now defined as YTH domain.
In previous studies, we found YTH domain of BC1 had ATPase activity which could hydrolyze ATP. In this thesis, we expressed and purified full-length BC1 and performed ATPase assay. Next, we tested N-terminal deletion and site-specific mutagenesis in YTH domain to understand the effect in ATPase activity, and the binding region of BC1 to ATP.
We also found when we transiently transfected EGFP-BC1 to cell, BC1 formed some small granule in cytosol. Cytosolic RNA-binding proteins are involved in RNA granule formation and transportation, which have closely relationship with tubulin, This thesis will investigate BC1 and the interaction with tubulin.
Subjects
ATPase
BC1
tubulin
granule
Type
other
File(s)![Thumbnail Image]()
Loading...
Name
ntu-94-R92b46028-1.pdf
Size
23.31 KB
Format
Adobe PDF
Checksum
(MD5):9545af387c61c2af7395bd1087a6259d