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Nucleic Acids Research, 1990, Vol. 18, No. 24 7299-7303
© 1990

Articles

A gene from the VSG expression site of Trypanosoma brucei encodes a protein with both leucine-rich repeats and a putative zinc finger

Philippe Revelard, Stéphane Lips and Etienne Pays*

Department of Molecular Biology, University of Brussels 67, rue des Chevaux, B1640 Rhode Saint Genèse, Belgium

*To whom correspondence should be addressed

Received September 24, 1990. Revised November 19, 1990. Accepted November 19, 1990.

The transcription unit of the gene for the variant specific glycoprotein (VSG) AnTat 1.3A of Trypanosoma brucel contains several associated genes (ESAGs, for Expression Site-Associated Genes), 7 of which have already been described (1). 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. ESA-G 8 transcripts are only found in bloostream 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.


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