RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1
Open accessAbstract
Genes for immunoglobulins and T-cell receptor are generated by a process known as V(D)J recombination. This process is highly regulated and mediated by the recombination activating proteins RAG-1 and RAG-2. By the use of the two-hybrid protein interaction system, we isolated a human protein that specifically interacts with RAG-1. This protein is the human homologue of the yeast SRP1 (suppressor of a temperature-sensitive RNA polymerase I mutation). The SRP1-1 mutation is an allele-specific dominant suppressor of a temperature-sensitive mutation in the zinc binding domain of the 190-kDa subunit of Saccharomyces cerevisiae RNA polymerase I. The human SRP cDNA clone was used to screen a mouse cDNA library. We obtained a 3.9-kbp cDNA clone encoding the mouse SRP1. The open reading frame of this cDNA encodes a 538-amino acid protein with eight degenerate repeats of 40-45 amino acids each. The mouse and human SRP1 are 98% identical, while the mouse and yeast SRP1 have 48% identity. After cotransfection of the genes encoding RAG-1 and human SRP1 into 293T cells, a stable complex was evident. Deletion analysis indicated that the region of the SRP1 protein interacting with RAG-1 involved four repeats. The domain of RAG-1 that associates with SRP1 mapped N-terminal to the zinc finger domain. Because this region of RAG-1 is not required for recombination and SRP1 appears to be bound to the nuclear envelope, we suggest that this interaction helps to localize RAG-1.
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“In humans, six importin-a isoforms are known [41,42,43,44].”
Background
- Authors
- Cortes, P., Ye, Z. S., & Baltimore, D.
- Affiliations
- Rockefeller University, New York, NY 10021.
- Rockefeller University (US)
- ORCID
- Baltimore, D
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1994-08-02
- Volume
- 91
- Issue
- 16
- Pages
- 7633-7637
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC44456
- OpenAlex
- W2001744377
- Cited by
- 173
- References
- 29
- Citations by year
- 2026: 2 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 1 · 2018: 1 · 2017: 1 · 2016: 3 · 2015: 2 · 2014: 3 · 2013: 3 · 2012: 2
- FWCI
- 7.59
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- National Cancer Institute (CA54162)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- RAG1, protein-protein interaction, V(D)J recombination, immunoglobulin gene rearrangement, T-cell receptor gene rearrangement, zinc finger, nuclear envelope localization, RNA polymerase I, Saccharomyces cerevisiae
- MeSH terms
- Amino Acid Sequence, Animals, DNA Mutational Analysis, Humans, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Proteins, Receptors, Antigen, T-Cell, Recombination, Genetic, Repetitive Sequences, Nucleic Acid, Saccharomyces cerevisiae, Structure-Activity Relationship, Gene Rearrangement, T-Lymphocyte, Sequence Homology, Amino Acid, Homeodomain Proteins, alpha Karyopherins, Mice
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