Hypermutation generating the sheep immunoglobulin repertoire is an antigen-independent process

Article Abstract:

Experimental studies of the somatic hypermutation of light chain V genes in the ileum of germ-free sheep, in thymectomized animals and in sterile ileum fragments isolated from gut reveal that the accumulation of the mutations on the genes is independent of external antigens and that the pattern of the mutations is similar in all the three experimental and in the control tissues. The hypermutation process targets the replacement mutations in the complimentarity-determining regions. The major V-lambda genes display codon usage specificity with high purine levels at the first two codon bases and low purine levels at the third base.

Antigens, Ileum

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The C. elegans ksr-1 gene encodes a novel Raf-related kinase involved in Ras-medicated signal transduction

Article Abstract:

The Caenorhabditis elegans kinase suppressor of RAS (KSR) is necessary for the signaling activity of activated let-60 ras and development of the multivulva (Muv) phenotype. Mutations in ksr-1 suppress the Muv phenotype. Mutant ksr-1 genes suppress the Muv phenotype due to mutant kuls12 gene. However, the mutant kuls13 phenotype remains unaffected. The KSR protein kinase is structurally similar to the Raf Ser/Thr kinases. The kinase acts between let-60 ras and the transcription factor lin-1.

Caenorhabditis elegans, Protein kinases

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The fourth immunoglobulin domain of the stem cell factor receptor couples ligand binding to signal transduction

Article Abstract:

Use of a dimerization-inhibitory monoclonal antibody (MAb) to stem cell factor (SCF) receptor helps identify the fourth immunoglobulin domain that is the site of dimerization of SCF receptor. Deletion of the new domain results in the suppression of signal transduction, prevention of ligand-induced dimerization and also provides information about the correlation between dimer formation and ligand binding. The experimental studies indicate the presence of similar sites in the receptor.f

Ligand binding (Biochemistry), Stem cells

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