当前位置： SCI文献检索 > MOLECULAR AND BIOCHEMICAL PARASITOLOGY期刊下所有文献 > Theileria parva 104 kDa microneme--rhoptry protein is membrane-anchored by a non-cleaved amino-terminal signal sequence for entry into the endoplasmic reticulum.

Theileria parva 104 kDa microneme--rhoptry protein is membrane-anchored by a non-cleaved amino-terminal signal sequence for entry into the endoplasmic reticulum.

Abstract：

:The 104 kDa microneme-rhoptry protein (p104) is the only known apical complex organelle-specific protein of Theileria parva. p104 exhibits striking structural similarities to circumsporozoite protein and sporozoite surface protein 2 of Plasmodium yoelii. Their primary sequences contain two hydrophobic segments, located at the amino-and the carboxy-terminus. The p104 amino-terminal hydrophobic region was suggested to be a signal peptide for entry into the endoplasmic reticulum and the extreme carboxy-terminal region to function as a membrane anchor. We have studied the biogenesis of p104 in a cell-free expression system and found that p104 is co-translationally transported into membranes derived from endoplasmic reticulum. The amino-terminal signal peptide is not cleaved off and anchors the protein in the membrane with the carboxy-terminal portion translocated into the lumen. We suggest that in vivo p104 is co-translationally integrated into the membrane of the endoplasmic reticulum, from where it is further transported to the microneme-rhoptry complex. Thus, p104 appears to be a suitable marker to study the development of micronemes and rhoptries in T. parva.

journal_name

Mol Biochem Parasitol

journal_title

Molecular and biochemical parasitology

authors

Ebel T,Gerhards J,Binder BR,Lipp J

doi

10.1016/s0166-6851(99)00020-1

subject

Has Abstract

pub_date

1999-05-15 00:00:00

pages

19-26

issue

1

eissn

0166-6851

issn

1872-9428

pii

S0166-6851(99)00020-1

journal_volume

100

pub_type

杂志文章

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