Functional Characterization of Three Aquaglyceroporins from Trypanosoma brucei in Osmoregulation and Glycerol Transport

2011 ◽  
Vol 27 (3-4) ◽  
pp. 411-420 ◽  
Author(s):  
Björn Bassarak ◽  
Nestor L. Uzcátegui ◽  
Caroline Schönfeld ◽  
Michael Duszenko
RNA ◽  
2012 ◽  
Vol 18 (10) ◽  
pp. 1846-1861 ◽  
Author(s):  
L. Kafkova ◽  
M. L. Ammerman ◽  
D. Faktorova ◽  
J. C. Fisk ◽  
S. L. Zimmer ◽  
...  

FEBS Letters ◽  
2010 ◽  
Vol 584 (13) ◽  
pp. 2901-2908 ◽  
Author(s):  
Jian Yuan Goh ◽  
Cheng-Yu Lai ◽  
Luuan Chin Tan ◽  
Daiwen Yang ◽  
Cynthia Y. He ◽  
...  

mBio ◽  
2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Hung Quang Dang ◽  
Qing Zhou ◽  
Veronica W. Rowlett ◽  
Huiqing Hu ◽  
Kyu Joon Lee ◽  
...  

ABSTRACT The basal body shares similar architecture with centrioles in animals and is involved in nucleating flagellar axonemal microtubules in flagellated eukaryotes. The early-branching Trypanosoma brucei possesses a motile flagellum nucleated from the basal body that consists of a mature basal body and an adjacent pro-basal body. Little is known about the basal body proteome and its roles in basal body biogenesis and flagellar axoneme assembly in T. brucei . Here, we report the identification of 14 conserved centriole/basal body protein homologs and 25 trypanosome-specific basal body proteins. These proteins localize to distinct subdomains of the basal body, and several of them form a ring-like structure surrounding the basal body barrel. Functional characterization of representative basal body proteins revealed distinct roles in basal body duplication/separation and flagellar axoneme assembly. Overall, this work identified novel proteins required for basal body duplication and separation and uncovered new functions of conserved basal body proteins in basal body duplication and separation, highlighting an unusual mechanism of basal body biogenesis and inheritance in this early divergent eukaryote. IMPORTANCE The basal body in the early-branching protozoan Trypanosoma brucei nucleates flagellum assembly and also regulates organelle segregation, cell morphogenesis, and cell division. However, the molecular composition and the assembly process of the basal body remain poorly understood. Here, we identify 14 conserved basal body proteins and 25 trypanosome-specific basal body proteins via bioinformatics, localization-based screening, and proximity-dependent biotin identification. We further localized these proteins to distinct subdomains of the basal body by using fluorescence microscopy and superresolution microscopy, discovered novel regulators of basal body duplication and separation, and uncovered new functions of conserved basal body proteins in basal body duplication and separation. This work lays the foundation for dissecting the mechanisms underlying basal body biogenesis and inheritance in T. brucei .


2006 ◽  
Vol 92 (6) ◽  
pp. 1152-1161 ◽  
Author(s):  
Sedrick Anderson ◽  
Candace Jones ◽  
Lipi Saha ◽  
Minu Chaudhuri

2020 ◽  
Vol 21 (2) ◽  
pp. 663 ◽  
Author(s):  
Farzana Sabir ◽  
Sara Gomes ◽  
Maria C. Loureiro-Dias ◽  
Graça Soveral ◽  
Catarina Prista

Plant Nodulin 26-like Intrinsic Proteins (NIPs) are multifunctional membrane channels of the Major Intrinsic Protein (MIP) family. Unlike other homologs, they have low intrinsic water permeability. NIPs possess diverse substrate selectivity, ranging from water to glycerol and to other small solutes, depending on the group-specific amino acid composition at aromatic/Arg (ar/R) constriction. We cloned three NIPs (NIP1;1, NIP5;1, and NIP6;1) from grapevine (cv. Touriga Nacional). Their expression in the membrane of aqy-null Saccharomyces cerevisiae enabled their functional characterization for water and glycerol transport through stopped-flow spectroscopy. VvTnNIP1;1 demonstrated high water as well as glycerol permeability, whereas VvTnNIP6;1 was impermeable to water but presented high glycerol permeability. Their transport activities were declined by cytosolic acidification, implying that internal-pH can regulate NIPs gating. Furthermore, an extension of C-terminal in VvTnNIP6;1M homolog, led to improved channel activity, suggesting that NIPs gating is putatively regulated by C-terminal. Yeast growth assays in the presence of diverse substrates suggest that the transmembrane flux of metalloids (As, B, and Se) and the heavy metal (Cd) are facilitated through grapevine NIPs. This is the first molecular and functional characterization of grapevine NIPs, providing crucial insights into understanding their role for uptake and translocation of small solutes, and extrusion of toxic compounds in grapevine.


2006 ◽  
Vol 2006 (Spring) ◽  
Author(s):  
Alexandra Wendler ◽  
Thorsten Irsch ◽  
R. Luise Krauth-Siegel

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