FUNCTION OF N-TERMINAL IMPORT SIGNALS IN TRYPANOSOME MICROBODIES

Citation
J. Blattner et al., FUNCTION OF N-TERMINAL IMPORT SIGNALS IN TRYPANOSOME MICROBODIES, FEBS letters, 360(3), 1995, pp. 310-314
Citations number
30
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
360
Issue
3
Year of publication
1995
Pages
310 - 314
Database
ISI
SICI code
0014-5793(1995)360:3<310:FONISI>2.0.ZU;2-T
Abstract
The glycosomes of trypanosomes are related to eukaryotic peroxisomes. For many glycosomal and peroxisomal proteins, a C-terminal SKL-like tr ipeptide known as PTS-1 serves as the targeting signal. For peroxisome s, a second N-terminal signal (PTS-2) was demonstrated on rat 3-ketoac yl-CoA thiolase. Several glycosomal proteins do not bear a PTS-1. One such protein, fructose bisphosphate aldolase, has a PTS-2 homology at its N-terminus. To find out whether the PTS-2 pathway exists in trypan osomes, we expressed chloramphenicol acetyltransferase fusion proteins bearing N-terminal segments of either rat thiolase or trypanosome ald olase. The mammalian PTS-2 clearly mediated glycosomal import. The ald olase N-terminus mediated import with variable efficiency depending on the length of the appended sequence. These results provide evidence f or the existence of the PTS-2 pathway in trypanosomes.