Functional characterization of DnaB helicase and its modulation by single-stranded DNA binding protein in Mycobacterium tuberculosis
Version of Record online: 23 JAN 2014
© 2014 FEBS
The FEBS Journal
Volume 281, Issue 4, pages 1256–1266, February 2014
How to Cite
Zhang, H., Zhang, Z., Yang, J. and He, Z.-G. (2014), Functional characterization of DnaB helicase and its modulation by single-stranded DNA binding protein in Mycobacterium tuberculosis. The FEBS Journal, 281: 1256–1266. doi: 10.1111/febs.12703
- Issue online: 17 FEB 2014
- Version of Record online: 23 JAN 2014
- Accepted manuscript online: 4 JAN 2014 06:54AM EST
- Manuscript Accepted: 23 DEC 2013
- Manuscript Revised: 16 DEC 2013
- Manuscript Received: 3 JUL 2013
- 973 Program. Grant Number: 2012CB518800
- National Natural Science Foundation of China. Grant Numbers: 31000021, 31025002 and 31121004
Fig. S1. Influence of the unpaired base numbers in the 5′ and 3′ tail on MtbDnaB helicase activity.
Fig. S2. Influence of the 5′ and 3′ tail on MtbDnaB helicase activity.
Fig. S3. Effect of time on DnaB helicase activity.
Fig. S4. Electrophoretic mobility shift assays for DNA binding activity of MtbSSB.
Fig. S5. Protein expression level of MtbDnaB by western blot analysis.
Fig. S6. Effect of SSB on enzymatic activities of MtbDnaB.
Fig. S7. ATPase activity of M. tuberculosis DnaB protein in the presence of increasing concentrations of DNA effector that differ in their secondary structure.
Fig. S8. Quantitative RT-PCR assays for expression levels of the ssb gene in BCG.
Fig. S9. Protein sequence alignment of homologous DnaB proteins.
Data S1. Purification of M. tuberculosis DnaB protein.
Table S1. The primers and nucleotide sequences used in this study.
Table S2. Plasmids and recombinant vectors used in this study.
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