Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motif-Reference-Cited by-同舟云学术

Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motif

Published:1995-05 Issue:4 Volume:16 Page:699-708
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:Mol Microbiol

Author:

Schröder Katja,Graumann Peter,Schnuchel Arndt,Holak Tad A.,Marahiel Mohamed A.

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2958.1995.tb02431.x/fullpdf

Reference41 articles.

1. Streptomyces contain a 7.0 kDa cold shock like protein

2. Suggestions for “safe” residue substitutions in site-directed mutagenesis

3. A role for transcription and FRGY2 in masking maternal mRNA within Xenopus oocytes

4. Mechanism of DNA binding to the gene 5 protein of bacteriophage fd

5. Mutations in an RNP1 consensus sequence of Rho protein reduce RNA binding affinity but facilitate helicase turnover.

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