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Nucleic acid and protein sequences of phosphocholine-binding light chains
The Journal of Experimental Medicine
|May 1, 1981
Summary
Researchers cloned an 18-kilobase DNA fragment encoding the S107 mouse immunoglobulin kappa light chain. The nucleotide sequence revealed identity to the T15 light chain and confirmed the use of the J1 joining segment.
Area of Science:
- Immunology
- Molecular Biology
- Genetics
Background:
- Immunoglobulin light chains are crucial components of the adaptive immune system.
- The S107 mouse immunoglobulin light chain is a well-characterized example used in immunological studies.
- Understanding the genetic basis of immunoglobulin diversity is fundamental to immunology.
Purpose of the Study:
- To clone and determine the complete nucleotide sequence of the S107 mouse immunoglobulin kappa light chain gene.
- To analyze the encoded amino acid sequence and compare it with known protein sequences.
- To identify the specific joining (J) gene segment involved in the rearrangement of the kappa light chain locus.
Main Methods:
- Cloning of an 18-kilobase DNA fragment from total cellular DNA.
- Determination of the complete nucleotide sequence of the kappa-chain variable-region gene.
- Direct sequence analysis to confirm the J gene segment usage.
Main Results:
- The complete nucleotide sequence of the S107 mouse kappa light chain variable-region gene was determined.
- The deduced amino acid sequence matched the T15 light chain protein sequence up to residue 88.
- Sequence analysis confirmed the utilization of the J1 joining segment in the active gene.
Conclusions:
- The study provides the complete nucleotide sequence of the S107 mouse immunoglobulin kappa light chain gene.
- The findings confirm the structural similarity between the S107 and T15 light chains at the protein level.
- The J1 joining segment is essential for generating the functional S107 kappa light chain.