Thermal dependency of RAG1 self-association propertiesReport as inadecuate




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BMC Biochemistry

, 9:5

First Online: 30 January 2008Received: 07 May 2007Accepted: 30 January 2008

Abstract

BackgroundFunctional immunoglobulin and T cell receptor genes are produced in developing lymphocytes by VDJ recombination. The initial site-specific DNA cleavage steps in this process are catalyzed by the VDJ recombinase, consisting of RAG1 and RAG2, which is directed to appropriate DNA cleavage sites by recognition of the conserved recombination signal sequence RSS. RAG1 contains both the active site and the RSS binding domains, although RAG2 is also required for DNA cleavage activity. An understanding of the physicochemical properties of the RAG proteins, their association, and their interaction with the RSS is not yet well developed.

ResultsHere, we further our investigations into the self-association properties of RAG1 by demonstrating that despite the presence of multiple RAG1 oligomers, only the dimeric form maintains the ability to interact with RAG2 and the RSS. However, facile aggregation of the dimeric form at physiological temperature may render this protein inactive in the absence of RAG2. Upon addition of RAG2 at 37°C, the preferentially stabilized VDJ recombinase:RSS complex contains a single dimer of RAG1.

ConclusionTogether these results confirm that the functional form of RAG1 in VDJ recombination is in the dimeric state, and that its stability under physiological conditions likely requires complex formation with RAG2. Additionally, in future structural and functional studies of RAG1, it will be important to take into account the temperature-dependent self-association properties of RAG1 described in this study.

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2091-9-5 contains supplementary material, which is available to authorized users.

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Author: Pallabi De - Shuying Zhao - Lori M Gwyn - LeAnn J Godderz - Mandy M Peak - Karla K Rodgers

Source: https://link.springer.com/article/10.1186/1471-2091-9-5







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