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J. Biol. Chem., Vol. 276, Issue 18, 15511-15518, May 4, 2001
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From the The cold shock protein CspB from
Bacillus subtilis binds T-based single-stranded DNA (ssDNA)
with high affinity (Lopez, M. M., Yutani, K., and Makhatadze,
G. I. (1999) J. Biol. Chem. 274, 33601-33608).
In this paper we report the results of CspB interactions with
non-homogeneous ssDNA templates containing continuous and non-continuous stretches of T bases. The analysis of CspB-ssDNA interactions was performed using fluorescence spectroscopy, analytical centrifugation and isothermal titration calorimetry. We show that (i)
there is a strong correlation between the CspB affinity and stoichiometry and the T content in the oligonucleotide that is independent of which other bases are incorporated into the sequence of
ssDNA; (ii) the binding properties of CspB to ssDNA templates with
continuous or non-continuous stretches of T bases with similar T
content is very similar, and (iii) the mechanism of interaction between
CspB and the T-based non-homogeneous ssDNA is mainly through the bases
(a stretch of three T bases located in the middle of the ssDNA
templates makes the binding independent of the ionic strength). The
biological relevance of these results to the role of CspB as an RNA
chaperone is discussed.
Interactions of the Cold Shock Protein CspB from
Bacillus subtilis with Single-stranded DNA
IMPORTANCE OF THE T BASE CONTENT AND POSITION WITHIN THE
TEMPLATE*
,¶
Department of Biochemistry and Molecular
Biology, Penn State University, College of Medicine, Hershey,
Pennsylvania 17033 and the § Institute for Protein Research,
Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan
*
This work was supported by Human Frontier in Science Program
Grant RPG-0036/1997M.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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