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Title: A gene from the VSG expression site of Trypanosoma brucei encodes a protein with both leucine-rich repeats and a putative zinc finger. Author: Revelard P, Lips S, Pays E. Journal: Nucleic Acids Res; 1990 Dec 25; 18(24):7299-303. PubMed ID: 2259625. Abstract: The transcription unit of the gene for the variant specific glycoprotein (VSG) AnTat 1.3A of Trypanosoma brucei contains several associated genes (ESAGs, for Expression Site-Associated Genes), 7 of which have already been described. We report here the characterization of a further ESAG, which we term ESAG 8, present 1 kb downstream from the putative adenylate cyclase gene ESAG 4. ESAG 8 encodes a 70 kd protein whose sequence indicates that it is probably not exposed at the cell surface. With the exception of the N-terminal domain which contains a presumptive DNA-binding zinc finger, the ESAG 8 protein consists exclusively of leucine-rich repeats of 23 amino acids, typical of protein-interacting domains such as the RAS-interacting region of the yeast adenylate cyclase. ESAG 8 transcripts are only found in bloodstream forms, and their level is particularly low, suggesting a high rate of degradation. The ESAG 8 protein may be involved in stage-specific regulatory processes, such as gene expression control or adenylate cyclase activation.[Abstract] [Full Text] [Related] [New Search]