scholarly journals Tim17 Updates: A Comprehensive Review of an Ancient Mitochondrial Protein Translocator

Biomolecules ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 1643
Author(s):  
Minu Chaudhuri ◽  
Chauncey Darden ◽  
Fidel Soto Gonzalez ◽  
Ujjal K. Singha ◽  
Linda Quinones ◽  
...  
Keyword(s):  
Trypanosoma Brucei ◽  
Protein Complexes ◽  
Mitochondrial Protein ◽  
Structure And Function ◽  
Parasitic Protozoan ◽  
Comprehensive Review ◽  
Subunit Protein ◽  
Yeast Fungi ◽  
And Function ◽  
Eukaryotic Supergroup

The translocases of the mitochondrial outer and inner membranes, the TOM and TIMs, import hundreds of nucleus-encoded proteins into mitochondria. TOM and TIMs are multi-subunit protein complexes that work in cooperation with other complexes to import proteins in different sub-mitochondrial destinations. The overall architecture of these protein complexes is conserved among yeast/fungi, animals, and plants. Recent studies have revealed unique characteristics of this machinery, particularly in the eukaryotic supergroup Excavata. Despite multiple differences, homologues of Tim17, an essential component of one of the TIM complexes and a member of the Tim17/Tim22/Tim23 family, have been found in all eukaryotes. Here, we review the structure and function of Tim17 and Tim17-containing protein complexes in different eukaryotes, and then compare them to the single homologue of this protein found in Trypanosoma brucei, a unicellular parasitic protozoan.

scholarly journals Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor

2006 ◽  
Vol 25 (19) ◽  
pp. 4675-4685 ◽  
Author(s):  
Dejana Mokranjac ◽  
Gleb Bourenkov ◽  
Kai Hell ◽  
Walter Neupert ◽  
Michael Groll
Keyword(s):  
Protein Import ◽  
Mitochondrial Protein ◽  
Structure And Function ◽  
Mitochondrial Protein Import ◽  
And Function

scholarly journals Structure of the TELO2-TTI1-TTI2 complex and its function in TOR recruitment to the R2TP chaperone

2020 ◽  
Author(s):  
Mohinder Pal ◽  
Hugo Muñoz-Hernandez ◽  
Dennis Bjorklund ◽  
Lihong Zhou ◽  
Gianluca Degliesposti ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Protein Complexes ◽  
Kinase Domain ◽  
Structure And Function ◽  
Pi3 Kinase ◽  
Rna Polymerases ◽  
Heat Repeat ◽  
And Function

AbstractThe R2TP (RUVBL1-RUVBL2-RPAP3-PIH1D1) complex, in collaboration with HSP90, functions as a chaperone for the assembly and stability of protein complexes, including RNA polymerases, snRNPs and PI3 kinase-like kinases (PIKK) such as TOR and SMG1. PIKK stabilisation depends on an additional complex of TELO2, TTI1 and TTI2 (TTT), whose structure and function are poorly understood. We have now determined the cryo-EM structure of the human R2TP-TTT complex that together with biochemical experiments reveals the mechanism of TOR recruitment to the R2TP-TTT chaperone. The HEAT-repeat TTT complex binds the kinase domain of TOR, without blocking its activity, and delivers TOR to the R2TP chaperone. In addition, TTT regulates the R2TP chaperone by inhibiting RUVBL1-RUVBL2 ATPase activity and by modulating the conformation and interactions of the PIH1D1 and RPAP3 components of R2TP. Together, our results show how TTT couples the recruitment of TOR to R2TP with the regulation of this chaperone system.

scholarly journals Structure and function of ADCK3, an ancient mitochondrial protein involved in coenzyme Q biosynthesis

2015 ◽  
Vol 29 (S1) ◽  
Author(s):  
Isabel Johnson ◽  
Jonathan Stefely ◽  
Andrew Reidenbach ◽  
David Pagliarini
Keyword(s):  
Coenzyme Q ◽  
Mitochondrial Protein ◽  
Structure And Function ◽  
And Function

Protozoan paradigms for cell biology

1999 ◽  
Vol 112 (17) ◽  
pp. 2797-2798 ◽  
Author(s):  
K. Vickerman ◽  
G.H. Coombs
Keyword(s):  
Trypanosoma Brucei ◽  
Cell Biology ◽  
Antigenic Variation ◽  
Leishmania Species ◽  
Structure And Function ◽  
Holistic View ◽  
And Function ◽  
The University ◽  
Regius Professor ◽  
Made In

This article introduces a miniseries of three commentaries on parasite cell biology. The reviews were written as a tribute to Keith Vickerman FRS on his retirement as Regius Professor of Zoology at the University of Glasgow and are based on presentations given at a symposium held to honour his pioneering work in the field. On page 2799 of this issue, Michael Ferguson reviews the structure and function of GPI anchors, and the contributions that studies of trypanosomes have made. In subsequent issues, James Alexander, Abhay Satoskar and David Russell discuss Leishmania species as models of intracellular parasitism, and Michael Turner presents a holistic view of antigenic variation in Trypanosoma brucei infections.

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