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Journal of Cell Science, Vol 88, Issue 1 47-55, Copyright © 1987 by Company of Biologists

JOURNAL ARTICLES

Isolation and characterization of a mutant of Tetrahymena thermophila blocked in secretion of lysosomal enzymes

P Hunseler, G Scheidgen-Kleyboldt and A Tiedtke
Institute of Zoology, University of Munster, FRG.

The development of a sensitive screening procedure for mutants of Tetrahymena thermophila blocked in secretion of lysosomal enzymes is described. By means of this procedure a mutant blocked in secretion of lysosomal enzymes has been isolated. This sec- mutant, MS-1, is constitutively blocked in release of at least six lysosomal enzymes, under both nutrient and non-nutrient conditions. MS-1 possesses, bound within the cell, the same amount of active lysosomal enzymes as the wild type. During starvation in media of low ionic strength MS-1 develops a highly vacuolated phenotype. This phenotype is caused by the sec- allele. It is reversed to a normal cell shape when the mutant is transferred to isotonic medium. The sec- mutant MS-1 contains mucocysts and is capable of inducing exocytosis of these secretory organelles, suggesting that Tetrahymena possesses at least two independent protein-secreting organelles.


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S. Melia, E. Cole, and A. Turkewitz
Mutational analysis of regulated exocytosis in Tetrahymena
J. Cell Sci., January 1, 1998; 111(1): 131 - 140.
[Abstract] [PDF]


© The Company of Biologists Ltd 1987