Disease relevance of Tsn

• Immunoblot analysis confirmed that the bacteriophage express Tsn on their surface [1].

High impact information on Tsn

• These findings demonstrate that Translin is expressed in neuronal dendrites and therefore support the hypothesis that the Translin/Trax complex may be involved in dendritic RNA processing [2].
• In situ hybridization studies demonstrated that both Translin and Trax are expressed in neurons with prominent staining apparent in cerebellar Purkinje cells and neuronal layers of the hippocampus [2].
• The gene III and VIII-encoded coat proteins (pIII and pVIII) from bacteriophage M13 have been fused to the C terminus of the serine protease, trypsin (Tsn) [1].
• Identification of Translin/Trax complex as a glucose response element binding protein in liver [3].
• The molar ratio of Translin/Trax in the polymers was 2:1 in the liver cytosols [3].

Anatomical context of Tsn

• Sequencing of peptides derived from these proteins led to their identification as Translin and Trax, interacting proteins identified in studies of DNA recombination in lymphocytes [4].
• Furthermore, immunohistochemical studies with Translin antibodies revealed prominent staining in Purkinje neuron cell bodies that extends into proximal and distal dendrites [2].

Physical interactions of Tsn

• Whether one or both of these proposed functions of the Translin/Trax complex explains the high basal level of GS1 binding activity present in the brain remains to be determined [4].

References