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PMID: 3104899 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

B lymphocyte-specific protein binding near an immunoglobulin kappa-chain gene J segment.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 84 ·No. 6 ·1987-03-00 ·Pages 1516-20

Weaver D, Baltimore D

Abstract

Nuclear extracts from pre-B and B cell lines contain a nuclear DNA binding protein (kappa locus protein, KLP) that specifically recognizes a DNA sequence in the immunoglobulin kappa light chain joining (J) segment gene region. KLP is not observed in mature B cells, T cells, or nonlymphoid cell types. Two tandem binding sites for KLP designated KI and KII have been identified by methylation interference analysis to be immediately proximal to the J kappa 1 nonamer-heptamer recognition sequences and separated by 38 base pairs from each other. Fragments of DNA containing KI and KII sites compete for binding to KLP, and both protein-DNA complexes have the same electrophoretic mobility. Other flanking sequences of immunoglobulin gene fragments do not bind to KLP. The position of KLP-DNA binding and its tissue-specific expression suggest that it may be involved in the regulation of lymphoid gene DNA rearrangements by targeting recombinase to the kappa-chain gene region.

MeSH Terms
Animals B-Lymphocytes/analysis Base Sequence Binding Sites Cell Line DNA/analysis DNA-Binding Proteins/analysis Immunoglobulin Variable Region/genetics Immunoglobulin kappa-Chains/genetics Methylation Mice Protein Binding Recombination, Genetic
Chemicals
DNA-Binding Proteins Immunoglobulin Variable Region Immunoglobulin kappa-Chains DNA
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Weaver D
Baltimore D
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.84.6.1516
Published
1987-03-00
Pages
1516-20
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC304465
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.84.6.1516 PMC Full Text View journal details
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