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Open Access Research article

Elucidating the domain architecture and functions of non-core RAG1: The capacity of a non-core zinc-binding domain to function in nuclear import and nucleic acid binding

Janeen L Arbuckle13, Negar S Rahman1, Shuying Zhao14, William Rodgers2 and Karla K Rodgers1*

Author affiliations

1 Department of Biochemistry and Molecular Biology, The University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73190, USA

2 Cardiovascular Biology Program, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104, USA

3 Department of Obstetrics and Gynecology, University of Alabama, Birmingham, Alabama 35294, USA

4 Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas 77030, USA

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Citation and License

BMC Biochemistry 2011, 12:23  doi:10.1186/1471-2091-12-23

Published: 20 May 2011

Abstract

Background

The repertoire of the antigen-binding receptors originates from the rearrangement of immunoglobulin and T-cell receptor genetic loci in a process known as V(D)J recombination. The initial site-specific DNA cleavage steps of this process are catalyzed by the lymphoid specific proteins RAG1 and RAG2. The majority of studies on RAG1 and RAG2 have focused on the minimal, core regions required for catalytic activity. Though not absolutely required, non-core regions of RAG1 and RAG2 have been shown to influence the efficiency and fidelity of the recombination reaction.

Results

Using a partial proteolysis approach in combination with bioinformatics analyses, we identified the domain boundaries of a structural domain that is present in the 380-residue N-terminal non-core region of RAG1. We term this domain the Central Non-core Domain (CND; residues 87-217).

Conclusions

We show how the CND alone, and in combination with other regions of non-core RAG1, functions in nuclear localization, zinc coordination, and interactions with nucleic acid. Together, these results demonstrate the multiple roles that the non-core region can play in the function of the full length protein.