Disease relevance of LOC395566

• Expression plasmids containing these cDNA variants produced large amounts of T-protein in Escherichia coli, while very low expression was observed with a plasmid containing wild type cDNA [1].
• However p59v-rel was able to cooperate in a synergistic way with the polyomavirus middle T protein in inducing efficient transformation of established rat fibroblasts by increasing the steady-state level of middle T RNA, indicating that p59v-rel might function as a transactivator [2].
• Polyomavirus middle T protein encoded by a retrovirus transforms nonestablished chicken embryo cells [3].

High impact information on LOC395566

• We previously discovered a cellular isoform of titin (originally named T-protein) colocalized with myosin II in the terminal web domain of the chicken intestinal epithelial cell brush border cytoskeleton (Eilertsen, K.J., and T.C.S. Keller. 1992. J. Cell Biol. 119:549-557) [4].
• To see whether an excess of p60c-src could alter the extent of phosphorylation of the middle T protein or the process of cell transformation by middle T, cells were doubly infected with SRMT1 and NY501, a virus which overexpresses p60c-src [5].
• DNA clones encoding chicken T-protein of the glycine cleavage system were isolated from chicken liver lambda gt10 cDNA libraries [1].
• NH2-terminal amino acid sequence analysis (9 residues) revealed 100% identity with chicken T-protein determined chemically [1].
• A cDNA encoding mature T-protein was constructed, and the nucleotide sequence just downstream of the initiation codon was modified without amino acid substitution to reduce the free energy of formation for the folded mRNA [1].

Chemical compound and disease context of LOC395566

• Molecular cloning of a cDNA encoding chicken T-protein of the glycine cleavage system and expression of the functional protein in Escherichia coli. Effect of mRNA secondary structure in the translational initiation region on expression [1].

Biological context of LOC395566

• The amino acid sequence predicted for the mature protein showed 67% identity with that of bovine T-protein [1].

Anatomical context of LOC395566

• Immunolocalization in cryosections of intestinal epithelia and SDS-PAGE analysis of fractionated brush borders revealed that both T-protein and N-protein are concentrated distinctly in the brush border terminal web region subjacent to the microvilli, but absent from the microvilli [6].
• T-protein, a component of the glycine cleavage system, has been purified to apparent homogeneity from chicken liver mitochondria [7].
• The photoreaction of AMT with hen oviduct mRNA appeared to occur in two phases - a rapid monoaddition followed by a slower conversion of monoadducts to diadducts (i.e. crosslinking) [8].

Associations of LOC395566 with chemical compounds

• In the absence of tetrahydrofolate, T-protein catalyzes the stoichiometric formation of ammonia and formaldehyde from the intermediate although the velocity is extremely low [9].
• 0. T-protein is a basic protein having a pI value of 9.8 and relatively rich in arginine rather than lysine [7].
• Ovalbumin-specific DNA primer extension was used to demonstrate the selective and secondary structure specific photoaddition of AMT to uracil bases at the 5' end of ovalbumin mRNA [8].

Analytical, diagnostic and therapeutic context of LOC395566

• The 33 amino acids immediately following the targeting sequence correspond exactly to those determined by sequence analysis of the amino terminus of the purified bovine T-protein [10].
• Southern blot analysis of genomic DNA suggested that T-protein is a single copy gene [10].

References