scholarly journals LAX28 is required for assembly of the inner dynein arm l1 and tether/tether head complex in the Leishmania flagellum

2019 ◽  
Author(s):  
Tom Beneke ◽  
Katherine Banecki ◽  
Sophia Fochler ◽  
Eva Gluenz
Keyword(s):  
Proteome Analysis ◽  
Human Sperm ◽  
Null Mutant ◽  
Flagellar Motility ◽  
Leishmania Mexicana ◽  
Dynein Motor ◽  
Associated Proteins ◽  
Tail Protein ◽  
Summary Statement ◽  
Bluf Domain

AbstractMotile eukaryotic flagella beat through coordinated activity of dynein motor proteins yet the mechanisms of dynein coordination and regulation are incompletely understood. The inner dynein arm IDA f/I1 complex and the tether/tether head (T/TH) complex are thought to be key regulators but, unlike IDA f/I1, T/TH proteins show limited conservation across flagellates. Here we characterised T/TH-associated proteins in the protist Leishmania mexicana. Proteome analysis of ΔCFAP44 mutant axonemes showed that they lacked IDA f/I1 protein IC140 and a novel 28-kDA axonemal protein, LAX28. Sequence analysis identified similarities between LAX28 and the uncharacterised human sperm tail protein TEX47, sharing features with sensory BLUF-domain proteins. Leishmania lacking LAX28, CFAP44 or IC140 retained some motility albeit with reduced swimming speed and directionality and a propensity for flagellar curling. Expression of tagged proteins in different null mutant backgrounds showed that the axonemal localisation of LAX28 requires CFAP44 and IC140, and the axonemal localisations of CFAP44 and IC140 both depend on LAX28. These data demonstrate a role for LAX28 in motility and show mutual dependencies of IDA f/1I and T/TH-associated proteins for axonemal assembly in Leishmania.Summary StatementThe inner dynein arm f/l1 complex is required for coordinating flagellar motility. Here we show that LAX28 is needed for its function and localization in the flagellum of Leishmania mexicana.

Proteome analysis of actin filament-associated proteins in the postnatal rat cerebellum

Neuroscience ◽  
2012 ◽  
Vol 227 ◽  
pp. 90-101 ◽  
Author(s):  
N. Shi ◽  
C. Tian ◽  
X. Liang ◽  
P. Jiang ◽  
L. Liang ◽  
...  
Keyword(s):  
Actin Filament ◽  
Proteome Analysis ◽  
Rat Cerebellum ◽  
Associated Proteins

Cold Acclimation Proteome Analysis Reveals Close Link between the Up-Regulation of Low-Temperature Associated Proteins and Vernalization Fulfillment

2010 ◽  
Vol 9 (11) ◽  
pp. 5658-5667 ◽  
Author(s):  
Elham Sarhadi ◽  
Siroos Mahfoozi ◽  
Seyed Abdollah Hosseini ◽  
Ghasem Hosseini Salekdeh
Keyword(s):  
Low Temperature ◽  
Cold Acclimation ◽  
Proteome Analysis ◽  
Close Link ◽  
Associated Proteins

Extraction and Proteome Analysis of Starch Granule-Associated Proteins in Mature Wheat Kernel (Triticum aestivumL.)

2010 ◽  
Vol 9 (6) ◽  
pp. 3299-3310 ◽  
Author(s):  
Emmanuelle Bancel ◽  
Hélène Rogniaux ◽  
Clément Debiton ◽  
Christophe Chambon ◽  
Gérard Branlard
Keyword(s):  
Starch Granule ◽  
Proteome Analysis ◽  
Wheat Kernel ◽  
Associated Proteins

Proteome analysis of microtubule-associated proteins and their interacting partners from mammalian brain

Amino Acids ◽  
2010 ◽  
Vol 41 (2) ◽  
pp. 363-385 ◽  
Author(s):  
Frank Kozielski ◽  
Tahira Riaz ◽  
Salvatore DeBonis ◽  
Christian J. Koehler ◽  
Mario Kroening ◽  
...  
Keyword(s):  
Proteome Analysis ◽  
Mammalian Brain ◽  
Microtubule Associated Proteins ◽  
Associated Proteins

scholarly journals Domains in the 1α Dynein Heavy Chain Required for Inner Arm Assembly and Flagellar Motility in Chlamydomonas

1999 ◽  
Vol 146 (4) ◽  
pp. 801-818 ◽  
Author(s):  
Steven H. Myster ◽  
Julie A. Knott ◽  
Katrina M. Wysocki ◽  
Eileen O'Toole ◽  
Mary E. Porter
Keyword(s):  
Heavy Chain ◽  
Motor Domain ◽  
Flagellar Motility ◽  
Phosphate Binding ◽  
Binding Motifs ◽  
Phototactic Behavior ◽  
Dynein Heavy Chain ◽  
Dynein Motor ◽  
Mutant Phenotypes

Flagellar motility is generated by the activity of multiple dynein motors, but the specific role of each dynein heavy chain (Dhc) is largely unknown, and the mechanism by which the different Dhcs are targeted to their unique locations is also poorly understood. We report here the complete nucleotide sequence of the Chlamydomonas Dhc1 gene and the corresponding deduced amino acid sequence of the 1α Dhc of the I1 inner dynein arm. The 1α Dhc is similar to other axonemal Dhcs, but two additional phosphate binding motifs (P-loops) have been identified in the NH2- and COOH-terminal regions. Because mutations in Dhc1 result in motility defects and loss of the I1 inner arm, a series of Dhc1 transgenes were used to rescue the mutant phenotypes. Motile cotransformants that express either full-length or truncated 1α Dhcs were recovered. The truncated 1α Dhc fragments lacked the dynein motor domain, but still assembled with the 1β Dhc and other I1 subunits into partially functional complexes at the correct axoneme location. Analysis of the transformants has identified the site of the 1α motor domain in the I1 structure and further revealed the role of the 1α Dhc in flagellar motility and phototactic behavior.

scholarly journals Characterization of the Novel Mitochondrial Genome Segregation Factor TAP110 in Trypanosoma brucei

2021 ◽  
pp. jcs.254300
Author(s):  
Simona Amodeo ◽  
Ana Kalichava ◽  
Albert Fradera-Sola ◽  
Eloïse Bertiaux-Lequoy ◽  
Paul Guichard ◽  
...  
Keyword(s):  
Mitochondrial Genome ◽  
Trypanosoma Brucei ◽  
Proteome Analysis ◽  
Protozoan Parasite ◽  
Eukaryotic Cell ◽  
The Novel ◽  
Precise Position ◽  
Associated Proteins ◽  
First Time

Proper mitochondrial genome inheritance is important for eukaryotic cell survival. Trypanosoma brucei, a protozoan parasite, contains a singular mitochondrial genome, the kDNA. The kDNA is anchored to the basal body via the tripartite attachment complex (TAC) to ensure proper segregation. Several components of the TAC have been described. However, the connection of the TAC to the kDNA remains elusive. Here, we characterize the TAC associated protein TAP110. Depletion as well as overexpression of TAP110 leads to a delay in the separation of the replicated kDNA networks. Proteome analysis after TAP110 overexpression identified several kDNA associated proteins including a TEX-like protein that dually localizes to the nucleus and the kDNA potentially linking replication/segregation in the two compartments. The assembly of TAP110 into the TAC region seems to require the TAC but not the kDNA itself, however once TAP110 has been assembled it also interacts with the kDNA. Finally, for the first time we use ultrastructure expansion microscopy in trypanosomes to reveal the precise position of TAP110 between TAC102 and the kDNA, showcasing the potential of this approach.

scholarly journals 3D structure and in situ arrangements of CatSper channel in the sperm flagellum

2021 ◽  
Author(s):  
Yanhe Zhao ◽  
Huafeng Wang ◽  
Caroline Wiesehoefer ◽  
Naman B Shah ◽  
Evan Reetz ◽  
...  
Keyword(s):  
Electron Tomography ◽  
3D Structure ◽  
Human Sperm ◽  
Structural Basis ◽  
Sperm Flagellum ◽  
Mammalian Sperm ◽  
Zigzag Pattern ◽  
Associated Proteins

The sperm calcium channel CatSper plays a central role in successful fertilization as a primary Ca2+ gateway into the sperm flagellum. However, the complex subunit composition of CatSper has impeded its reconstitution in vitro and structural elucidation. Here, we applied cryo-electron tomography to visualize the macromolecular organization of the native CatSper channel complex in intact mammalian sperm, as well as identified three additional CatSper-associated proteins. The repeating CatSper units form long zigzag-rows in four nanodomains along the flagella. In both mouse and human sperm, each CatSper repeat consists of a tetrameric pore complex. Murine CatSper contains an additional outwardly directed wing-structure connected to the tetrameric channel. The majority of the extracellular domains form a canopy above each pore-forming channel that interconnects to a zigzag-shaped roof. The intracellular domains link two neighboring channel complexes to a diagonal array. The loss of this intracellular link in Efcab9-/- sperm distorts the longitudinally aligned zigzag pattern and compromises flagellar movement. This work offers unique insights into the mechanisms underlying the assembly and transport of the CatSper complex to generate the nanodomains and provides a long-sought structural basis for understanding CatSper function in the regulation of sperm motility.

scholarly journals ATP Production inChlamydomonas reinhardtiiFlagella by Glycolytic Enzymes

2005 ◽  
Vol 16 (10) ◽  
pp. 4509-4518 ◽  
Author(s):  
Beth F. Mitchell ◽  
Lotte B. Pedersen ◽  
Michael Feely ◽  
Joel L. Rosenbaum ◽  
David R. Mitchell
Keyword(s):  
Pyruvate Kinase ◽  
Atp Synthesis ◽  
Phosphoglycerate Mutase ◽  
Flagellar Motility ◽  
Atp Production ◽  
Dynein Motor ◽  
A Subunit ◽  
Cilia And Flagella

Eukaryotic cilia and flagella are long, thin organelles, and diffusion from the cytoplasm may not be able to support the high ATP concentrations needed for dynein motor activity. We discovered enzyme activities in the Chlamydomonas reinhardtii flagellum that catalyze three steps of the lower half of glycolysis (phosphoglycerate mutase, enolase, and pyruvate kinase). These enzymes can generate one ATP molecule for every substrate molecule consumed. Flagellar fractionation shows that enolase is at least partially associated with the axoneme, whereas phosphoglycerate mutase and pyruvate kinase primarily reside in the detergent-soluble (membrane + matrix) compartments. We further show that axonemal enolase is a subunit of the CPC1 central pair complex and that reduced flagellar enolase levels in the cpc1 mutant correlate with the reduced flagellar ATP concentrations and reduced in vivo beat frequencies reported previously in the cpc1 strain. We conclude that in situ ATP synthesis throughout the flagellar compartment is essential for normal flagellar motility.

scholarly journals Protein kinase C is present in human sperm: possible role in flagellar motility.

1990 ◽  
Vol 87 (18) ◽  
pp. 7305-7308 ◽  
Author(s):  
R Rotem ◽  
G F Paz ◽  
Z T Homonnai ◽  
M Kalina ◽  
Z Naor
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Sperm ◽  
Flagellar Motility ◽  
Kinase C
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