Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach

We have developed a novel DNA microarray-based approach for identification of the sequence-specificity of single-stranded nucleic-acid-binding proteins (SNABPs). For verification, we have shown that the major cold shock protein (CspB) from Bacillus subtilis binds with high affinity to pyrimidine-ric...

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Main Authors: Morgan, Hugh P., Estibeiro, Peter, Wear, Martin A., Max, Klaas E.A., Heinemann, Udo, Cubeddu, Liza, Gallagher, Maurice P., Sadler, Peter J., Walkinshaw, Malcolm D.
Format: Online
Language:English
Published: Oxford University Press 2007
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1904285/
id pubmed-1904285
recordtype oai_dc
spelling pubmed-19042852007-07-03 Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach Morgan, Hugh P. Estibeiro, Peter Wear, Martin A. Max, Klaas E.A. Heinemann, Udo Cubeddu, Liza Gallagher, Maurice P. Sadler, Peter J. Walkinshaw, Malcolm D. Methods Online We have developed a novel DNA microarray-based approach for identification of the sequence-specificity of single-stranded nucleic-acid-binding proteins (SNABPs). For verification, we have shown that the major cold shock protein (CspB) from Bacillus subtilis binds with high affinity to pyrimidine-rich sequences, with a binding preference for the consensus sequence, 5′-GTCTTTG/T-3′. The sequence was modelled onto the known structure of CspB and a cytosine-binding pocket was identified, which explains the strong preference for a cytosine base at position 3. This microarray method offers a rapid high-throughput approach for determining the specificity and strength of ss DNA–protein interactions. Further screening of this newly emerging family of transcription factors will help provide an insight into their cellular function. Oxford University Press 2007-05 2007-05-08 /pmc/articles/PMC1904285/ /pubmed/17488853 http://dx.doi.org/10.1093/nar/gkm040 Text en © 2007 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Morgan, Hugh P.
Estibeiro, Peter
Wear, Martin A.
Max, Klaas E.A.
Heinemann, Udo
Cubeddu, Liza
Gallagher, Maurice P.
Sadler, Peter J.
Walkinshaw, Malcolm D.
spellingShingle Morgan, Hugh P.
Estibeiro, Peter
Wear, Martin A.
Max, Klaas E.A.
Heinemann, Udo
Cubeddu, Liza
Gallagher, Maurice P.
Sadler, Peter J.
Walkinshaw, Malcolm D.
Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach
author_facet Morgan, Hugh P.
Estibeiro, Peter
Wear, Martin A.
Max, Klaas E.A.
Heinemann, Udo
Cubeddu, Liza
Gallagher, Maurice P.
Sadler, Peter J.
Walkinshaw, Malcolm D.
author_sort Morgan, Hugh P.
title Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach
title_short Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach
title_full Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach
title_fullStr Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach
title_full_unstemmed Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach
title_sort sequence specificity of single-stranded dna-binding proteins: a novel dna microarray approach
description We have developed a novel DNA microarray-based approach for identification of the sequence-specificity of single-stranded nucleic-acid-binding proteins (SNABPs). For verification, we have shown that the major cold shock protein (CspB) from Bacillus subtilis binds with high affinity to pyrimidine-rich sequences, with a binding preference for the consensus sequence, 5′-GTCTTTG/T-3′. The sequence was modelled onto the known structure of CspB and a cytosine-binding pocket was identified, which explains the strong preference for a cytosine base at position 3. This microarray method offers a rapid high-throughput approach for determining the specificity and strength of ss DNA–protein interactions. Further screening of this newly emerging family of transcription factors will help provide an insight into their cellular function.
publisher Oxford University Press
publishDate 2007
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1904285/
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