| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7557459 | Analytical Biochemistry | 2016 | 10 Pages |
Abstract
The DnaB helicase from Bacillus stearothermophilus (DnaBBst) was a model protein for studying the bacterial DNA replication. In this work, a non-radioactive method for measuring ATPase activity of DnaBBst helicase was described. The working parameters and conditions were optimized. Furthermore, this method was applied to investigate effects of DnaG primase, ssDNA and helicase loader protein (DnaI) on ATPase activity of DnaBBst. Our results showed this method was sensitive and efficient. Moreover, it is suitable for the investigation of functional interaction between DnaB and related factors.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Mu Yang, Ganggang Wang,