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Noncovalent protein interaction with poly(ADP-ribose)


Althaus, F R; Malanga, M (2011). Noncovalent protein interaction with poly(ADP-ribose). In: Tulin, A V. Poly(ADP-ribose) Polymerase. Methods and Protocols. New York: Springer, 67-82.

Abstract

Compared to most common posttranslational modifications of proteins, a peculiarity of poly(ADP-ribosyl)ation is the molecular heterogeneity and complexity of the reaction product, poly(ADP-ribose) (PAR). In fact, protein-bound PAR consists of variously sized (2-200 ADP-ribose residues) linear or branched molecules, negatively charged at physiological pH. It is now clear that PAR not only affects the function of the polypeptide to which it is covalently bound, but it can also influence the activity of other proteins by engaging specific noncovalent interactions. In the last 10 years, the family of PAR-binding proteins has been rapidly growing and functional studies have expanded the regulatory potential of noncovalent -protein targeting by PAR far beyond initial assumptions.In this chapter, methods are described for: (1) PAR synthesis and analysis; (2) detecting PAR-binding proteins in protein mixtures; (3) defining affinity and specificity of PAR binding to individual proteins or protein fragments; and (4) identifying PAR molecules selectively involved in the interaction.

Compared to most common posttranslational modifications of proteins, a peculiarity of poly(ADP-ribosyl)ation is the molecular heterogeneity and complexity of the reaction product, poly(ADP-ribose) (PAR). In fact, protein-bound PAR consists of variously sized (2-200 ADP-ribose residues) linear or branched molecules, negatively charged at physiological pH. It is now clear that PAR not only affects the function of the polypeptide to which it is covalently bound, but it can also influence the activity of other proteins by engaging specific noncovalent interactions. In the last 10 years, the family of PAR-binding proteins has been rapidly growing and functional studies have expanded the regulatory potential of noncovalent -protein targeting by PAR far beyond initial assumptions.In this chapter, methods are described for: (1) PAR synthesis and analysis; (2) detecting PAR-binding proteins in protein mixtures; (3) defining affinity and specificity of PAR binding to individual proteins or protein fragments; and (4) identifying PAR molecules selectively involved in the interaction.

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Additional indexing

Item Type:Book Section, refereed, original work
Communities & Collections:05 Vetsuisse Faculty > Institute of Veterinary Pharmacology and Toxicology
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:2011
Deposited On:28 Feb 2012 07:44
Last Modified:14 Sep 2016 13:46
Publisher:Springer
Series Name:Methods in Molecular Biology
Number:780
ISSN:1064-3745
ISBN:978-1-61779-270-0
Publisher DOI:https://doi.org/10.1007/978-1-61779-270-0_5
Related URLs:http://www.recherche-portal.ch/primo_library/libweb/action/search.do?fn=search&mode=Advanced&vid=ZAD&vl%28186672378UI0%29=isbn&vl%281UI0%29=contains&vl%28freeText0%29=978-1-61779-270-0
PubMed ID:21870255
Permanent URL: https://doi.org/10.5167/uzh-59839

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