scholarly journals SH3Ps—Evolution and Diversity of a Family of Proteins Engaged in Plant Cytokinesis

2019 ◽  
Vol 20 (22) ◽  
pp. 5623 ◽  
Author(s):  
Anežka Baquero Forero ◽  
Fatima Cvrčková
Keyword(s):  
Cell Plate ◽  
Yeast Two Hybrid ◽  
Microtubule Organization ◽  
Bar Domain ◽  
Plant Cytokinesis ◽  
Membrane Cytoskeleton ◽  
Yeast Two Hybrid System ◽  
Evolutionarily Conserved ◽  
Two Hybrid

SH3P2 (At4g34660), an Arabidopsis thaliana SH3 and Bin/amphiphysin/Rvs (BAR) domain-containing protein, was reported to have a specific role in cell plate assembly, unlike its paralogs SH3P1 (At1g31440) and SH3P3 (At4g18060). SH3P family members were also predicted to interact with formins—evolutionarily conserved actin nucleators that participate in microtubule organization and in membrane–cytoskeleton interactions. To trace the origin of functional specialization of plant SH3Ps, we performed phylogenetic analysis of SH3P sequences from selected plant lineages. SH3Ps are present in charophytes, liverworts, mosses, lycophytes, gymnosperms, and angiosperms, but not in volvocal algae, suggesting association of these proteins with phragmoplast-, but not phycoplast-based cell division. Separation of three SH3P clades, represented by SH3P1, SH3P2, and SH3P3 of A. thaliana, appears to be a seed plant synapomorphy. In the yeast two hybrid system, Arabidopsis SH3P3, but not SH3P2, binds the FH1 and FH2 domains of the formin FH5 (At5g54650), known to participate in cytokinesis, while an opposite binding specificity was found for the dynamin homolog DRP1A (At5g42080), confirming earlier findings. This suggests that the cytokinetic role of SH3P2 is not due to its interaction with FH5. Possible determinants of interaction specificity of SH3P2 and SH3P3 were identified bioinformatically.

scholarly journals Functional characterization of the KNOLLE-interacting t-SNARE AtSNAP33 and its role in plant cytokinesis

2001 ◽  
Vol 155 (2) ◽  
pp. 239-250 ◽  
Author(s):  
Maren Heese ◽  
Xavier Gansel ◽  
Liliane Sticher ◽  
Peter Wick ◽  
Markus Grebe ◽  
...  
Keyword(s):  
Cell Division ◽  
Membrane Fusion ◽  
Functional Characterization ◽  
Cell Plate ◽  
Yeast Two Hybrid ◽  
Division Plane ◽  
Plant Cytokinesis ◽  
Cell Plate Formation ◽  
Plate Formation ◽  
Two Hybrid

Cytokinesis requires membrane fusion during cleavage-furrow ingression in animals and cell plate formation in plants. In Arabidopsis, the Sec1 homologue KEULE (KEU) and the cytokinesis-specific syntaxin KNOLLE (KN) cooperate to promote vesicle fusion in the cell division plane. Here, we characterize AtSNAP33, an Arabidopsis homologue of the t-SNARE SNAP25, that was identified as a KN interactor in a yeast two-hybrid screen. AtSNAP33 is a ubiquitously expressed membrane-associated protein that accumulated at the plasma membrane and during cell division colocalized with KN at the forming cell plate. A T-DNA insertion in the AtSNAP33 gene caused loss of AtSNAP33 function, resulting in a lethal dwarf phenotype. atsnap33 plantlets gradually developed large necrotic lesions on cotyledons and rosette leaves, resembling pathogen-induced cellular responses, and eventually died before flowering. In addition, mutant seedlings displayed cytokinetic defects, and atsnap33 in combination with the cytokinesis mutant keu was embryo lethal. Analysis of the Arabidopsis genome revealed two further SNAP25-like proteins that also interacted with KN in the yeast two-hybrid assay. Our results suggest that AtSNAP33, the first SNAP25 homologue characterized in plants, is involved in diverse membrane fusion processes, including cell plate formation, and that AtSNAP33 function in cytokinesis may be replaced partially by other SNAP25 homologues.

scholarly journals The Rice Tungro Bacilliform Virus Gene II Product Interacts with the Coat Protein Domain of the Viral Gene III Polyprotein

2000 ◽  
Vol 74 (5) ◽  
pp. 2073-2083 ◽  
Author(s):  
Etienne Herzog ◽  
Orlene Guerra-Peraza ◽  
Thomas Hohn
Keyword(s):  
Coat Protein ◽  
Protein Domain ◽  
Rice Tungro Bacilliform Virus ◽  
Viral Gene ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Genes Encoding ◽  
Two Hybrid

ABSTRACT Rice tungro bacilliform virus (RTBV) is a plant pararetrovirus whose DNA genome contains four genes encoding three proteins and a large polyprotein. The function of most of the viral proteins is still unknown. To investigate the role of the gene II product (P2), we searched for interactions between this protein and other RTBV proteins. P2 was shown to interact with the coat protein (CP) domain of the viral gene III polyprotein (P3) both in the yeast two-hybrid system and in vitro. Domains involved in the P2-CP association have been identified and mapped on both proteins. To determine the importance of this interaction for viral multiplication, the infectivity of RTBV gene II mutants was investigated by agroinoculation of rice plants. The results showed that virus viability correlates with the ability of P2 to interact with the CP domain of P3. This study suggests that P2 could participate in RTBV capsid assembly.

scholarly journals Role of the Carboxy Terminus of Escherichia coli FtsA in Self-Interaction and Cell Division

2000 ◽  
Vol 182 (22) ◽  
pp. 6366-6373 ◽  
Author(s):  
Lucía Yim ◽  
Guy Vandenbussche ◽  
Jesús Mingorance ◽  
Sonsoles Rueda ◽  
Mercedes Casanova ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Biological Function ◽  
Wild Type ◽  
Carboxy Terminus ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Carboxy Terminal ◽  
Two Hybrid

ABSTRACT The role of the carboxy terminus of the Escherichia coli cell division protein FtsA in bacterial division has been studied by making a series of short sequential deletions spanning from residue 394 to 420. Deletions as short as 5 residues destroy the biological function of the protein. Residue W415 is essential for the localization of the protein into septal rings. Overexpression of theftsA alleles harboring these deletions caused a coiled cell phenotype previously described for another carboxy-terminal mutation (Gayda et al., J. Bacteriol. 174:5362–5370, 1992), suggesting that an interaction of FtsA with itself might play a role in its function. The existence of such an interaction was demonstrated using the yeast two-hybrid system and a protein overlay assay. Even these short deletions are sufficient for impairing the interaction of the truncated FtsA forms with the wild-type protein in the yeast two-hybrid system. The existence of additional interactions between FtsA molecules, involving other domains, can be postulated from the interaction properties shown by the FtsA deletion mutant forms, because although unable to interact with the wild-type and with FtsAΔ1, they can interact with themselves and cross-interact with each other. The secondary structures of an extensive deletion, FtsAΔ27, and the wild-type protein are indistinguishable when analyzed by Fourier transform infrared spectroscopy, and moreover, FtsAΔ27 retains the ability to bind ATP. These results indicate that deletion of the carboxy-terminal 27 residues does not alter substantially the structure of the protein and suggest that the loss of biological function of the carboxy-terminal deletion mutants might be related to the modification of their interacting properties.

Rab6 interacts with the mint3 adaptor protein

2005 ◽  
Vol 386 (7) ◽  
pp. 671-677 ◽  
Author(s):  
Iskender Teber ◽  
Fumiko Nagano ◽  
Joachim Kremerskothen ◽  
Konstantinos Bilbilis ◽  
Bruno Goud ◽  
...  
Keyword(s):  
Gradient Centrifugation ◽  
Adaptor Protein ◽  
Retrograde Transport ◽  
Effector Proteins ◽  
Yeast Two Hybrid ◽  
Golgi Membranes ◽  
Yeast Two Hybrid System ◽  
App Trafficking ◽  
Two Hybrid

Abstract The Rab6 GTPase regulates a retrograde transport route connecting endosomes and the endoplasmic reticulum (ER) via the Golgi apparatus. Recently it was shown that active (GTP-loaded) Rab6A regulates intracellular processing of the amyloid precursor protein (APP). To characterize the role of Rab6A in APP trafficking and to identify effector proteins of the active Rab6A protein, we screened a human placenta cDNA library using the yeast two-hybrid system. We isolated an interacting cDNA clone encoding part of the adaptor protein mint3. The interaction between Rab6A and mint3 is GTP-dependent and requires the complete phosphotyrosine-binding (PTB) domain of the mint protein, which also mediates the association with APP. By confocal microscopy we show that Rab6A, mint3 and APP co-localize at Golgi membranes in HeLa cells. Density gradient centrifugation of cytosolic extracts confirms a common distribution of these three proteins. Our data suggest that mint3 links Rab6A to APP traffic.

Characterization of plant proteins that interact with cowpea mosaic virus ‘60K’ protein in the yeast two-hybrid system

2002 ◽  
Vol 83 (4) ◽  
pp. 885-893 ◽  
Author(s):  
Jan E. Carette ◽  
Jan Verver ◽  
Joost Martens ◽  
Tony van Kampen ◽  
Joan Wellink ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Close Association ◽  
Cowpea Mosaic Virus ◽  
Yeast Two Hybrid ◽  
Host Proteins ◽  
Hybrid Search ◽  
Yeast Two Hybrid System ◽  
Two Hybrid

Cowpea mosaic virus (CPMV) replication occurs in close association with small membranous vesicles in the host cell. The CPMV RNA1-encoded 60 kDa nucleotide-binding protein (‘60K’) plays a role in the formation of these vesicles. In this study, five cellular proteins were identified that interacted with different domains of 60K using a yeast two-hybrid search of an Arabidopsis cDNA library. Two of these host proteins (termed VAP27-1 and VAP27-2), with high homology to the VAP33 family of SNARE-like proteins from animals, interacted specifically with the C-terminal domain of 60K and upon transient expression colocalized with 60K in CPMV-infected cowpea protoplasts. eEF1-β, picked up using the central domain of 60K, was also found to colocalize with 60K. The possible role of these host proteins in the viral replicative cycle is discussed.

Platelet Septins: Interaction of the Human Septins SEPT5, SEPT7 and SEPT11.

Blood ◽  
2007 ◽  
Vol 110 (11) ◽  
pp. 3891-3891
Author(s):  
Barbara Zieger ◽  
Ingrid Bartsch ◽  
Susanne Bläser ◽  
Busse Anja ◽  
Sabrina Roeseler ◽  
...  
Keyword(s):  
Human Platelets ◽  
Yeast Two Hybrid ◽  
Platelet Surface ◽  
Yeast Two Hybrid System ◽  
Serotonin Secretion ◽  
Transmission Electron ◽  
Interaction Partners ◽  
Dividing Cells ◽  
Two Hybrid

Abstract Septins are GTP-binding proteins which form heteropolymeric complexes. In non-dividing cells (such as platelets and neurons) septins are implicated in exocytosis. The SEPT4, SEPT5 and SEPT8 are expressed in platelets. Platelets from a SEPT5 knockout mouse showed an altered serotonin secretion and platelet aggregation suggesting that SEPT5 is involved in secretion in platelets. Transmission electron microscopy of platelets revealed that SEPT4, SEPT5 and SEPT8 are localized surrounding alpha-granules suggesting that the three septins may be components of the septin complex in platelets and contribute in such a way to platelet biology. Activation of platelets by agonists resulted in the translocation of SEPT4 and SEPT8 to the platelet surface indicating a possible functional role of these proteins in granular secretion. Previously, we identified the interaction of SEPT5 with SEPT8 and showed that SEPT5 partners with SEPT11. The aim of this study was to identify other interaction partners of SEPT11. Using the yeast two-hybrid system we demonstrate that SEPT11 partners with SEPT7. Western analysis revealed that SEPT7 is also expressed in platelets. The molecular interaction of SEPT11 with SEPT7 was verified by precipitation of the SEPT7/SEPT11 complex from lysates of human platelets. Since SEPT5, SEPT7 and SEPT11 are members of the same septin complex and since SEPT5, SEPT7 and SEPT11 are expressed in platelets, SEPT5, SEPT7 and SEPT11 may play an important role in exocytosis in platelets.

Identifications of DNA Sequences Encoding Key Region of SCR Interacting with SRK Extracellular Domain by Using Yeast Two-Hybrid System

2013 ◽  
Vol 38 (9) ◽  
pp. 1583-1591
Author(s):  
Li-Yan XUE ◽  
Bing LUO ◽  
Li-Quan ZHU ◽  
Yong-Jun YANG ◽  
He-Cui ZHANG ◽  
...  
Keyword(s):  
Hybrid System ◽  
Dna Sequences ◽  
Extracellular Domain ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Two Hybrid

scholarly journals Implication of the Whitefly Protein Vps Twenty Associated 1 (Vta1) in the Transmission of Cotton Leaf Curl Multan Virus

2021 ◽  
Vol 9 (2) ◽  
pp. 304
Author(s):  
Yao Chi ◽  
Li-Long Pan ◽  
Shu-Sheng Liu ◽  
Shahid Mansoor ◽  
Xiao-Wei Wang
Keyword(s):  
Coat Protein ◽  
Molecular Mechanisms ◽  
Cotton Leaf ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Vacuolar Protein ◽  
Leaf Curl Disease ◽  
Two Hybrid ◽  
Asia Ii 1 ◽  
Leaf Curl

Cotton leaf curl Multan virus (CLCuMuV) is one of the major casual agents of cotton leaf curl disease. Previous studies show that two indigenous whitefly species of the Bemisia tabaci complex, Asia II 1 and Asia II 7, are able to transmit CLCuMuV, but the molecular mechanisms underlying the transmission are poorly known. In this study, we attempted to identify the whitefly proteins involved in CLCuMuV transmission. First, using a yeast two-hybrid system, we identified 54 candidate proteins of Asia II 1 that putatively can interact with the coat protein of CLCuMuV. Second, we examined interactions between the CLCuMuV coat protein and several whitefly proteins, including vacuolar protein sorting-associated protein (Vps) twenty associated 1 (Vta1). Third, using RNA interference, we found that Vta1 positively regulated CLCuMuV acquisition and transmission by the Asia II 1 whitefly. In addition, we showed that the interaction between the CLCuMuV coat protein and Vta1 from the whitefly Middle East-Asia Minor (MEAM1), a poor vector of CLCuMuV, was much weaker than that between Asia II 1 Vta1 and the CLCuMuV coat protein. Silencing of Vta1 in MEAM1 did not affect the quantity of CLCuMuV acquired by the whitefly. Taken together, our results suggest that Vta1 may play an important role in the transmission of CLCuMuV by the whitefly.

Sign in / Sign up

Export Citation Format

Share Document