Characterization of glycosomal RING finger proteins of trypanosomatids.

Abstract:

:The glycosomes of trypanosomatids are essential organelles that are evolutionarily related to peroxisomes of other eukaryotes. The peroxisomal RING proteins-PEX2, PEX10 and PEX12-comprise a network of integral membrane proteins that function in the matrix protein import cycle. Here, we describe PEX10 and PEX12 in Trypanosoma brucei, Leishmania major, and Trypanosoma cruzi. We expressed GFP fusions of each T. brucei coding region in procyclic form T. brucei, where they localized to glycosomes and behaved as integral membrane proteins. Despite the weak transmembrane predictions for TbPEX12, protease protection assays demonstrated that both the N and C termini are cytosolic, similar to mammalian PEX12. GFP fusions of T. cruzi PEX10 and L. major PEX12 also localized to glycosomes in T. brucei indicating that glycosomal membrane protein targeting is conserved across trypanosomatids.

journal_name

Exp Parasitol

authors

Saveria T,Kessler P,Jensen BC,Parsons M

doi

10.1016/j.exppara.2006.11.004

subject

Has Abstract

pub_date

2007-05-01 00:00:00

pages

14-24

issue

1

eissn

0014-4894

issn

1090-2449

pii

S0014-4894(06)00295-5

journal_volume

116

pub_type

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