A leucine aminopeptidase is involved in kinetoplast DNA segregation in Trypanosoma brucei

PLoS Pathogens

Christian Resl¹  Mark C. Field¹  Marie Vancová²  Priscila Peña-Diaz²  Julius Lukeš³ 

[1] Faculty of Science, University of South Bohemia, České Budějovice (Budweis), Czech Republic;Institute of Parasitology, Biology Centre, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic;School of Life Sciences, University of Dundee, Dundee, United Kingdom

关键词: Kinetoplasts;    Cell cycle;    cell division;    Trypanosoma;    Trypanosoma brucei gambiense;    Sequence alignment;    DNA replication;    RNA interference;    Trypanosoma brucei;   

DOI  :  10.1371/journal.ppat.1006310

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

The kinetoplast (k), the uniquely packaged mitochondrial DNA of trypanosomatid protists is formed by a catenated network of minicircles and maxicircles that divide and segregate once each cell cycle. Although many proteins involved in kDNA replication and segregation are now known, several key steps in the replication mechanism remain uncharacterized at the molecular level, one of which is the nabelschnur or umbilicus, a prominent structure which in the mammalian parasite Trypanosoma brucei connects the daughter kDNA networks prior to their segregation. Here we characterize an M17 family leucyl aminopeptidase metalloprotease, termed TbLAP1, which specifically localizes to the kDNA disk and the nabelschur and represents the first described protein found in this structure. We show that TbLAP1 is required for correct segregation of kDNA, with knockdown resulting in delayed cytokinesis and ectopic expression leading to kDNA loss and decreased cell proliferation. We propose that TbLAP1 is required for efficient kDNA division and specifically participates in the separation of daughter kDNA networks.

【 授权许可】

CC BY