Planta, volume 245, issue 1, pages 193-205
Plant-specific 4/1 polypeptide interacts with an endoplasmic reticulum protein related to human BAP31
Pankratenko Anna V
1
,
Atabekova Anastasia K
1
,
Lazareva Ekaterina A.
1
,
Baksheeva Viktoriia E.
2
,
Zernii Evgeni Yu.
2
,
Owens Robert A.
3
,
Solovyev Andrey G.
2, 4
,
Morozov Sergey Y.
1, 2
3
Molecular Plant Pathology Laboratory, USDA-ARS, Beltsville, USA
|
Publication type: Journal Article
Publication date: 2016-10-06
Genetics
Plant Science
Abstract
AbstractMain conclusionThe plant-specific 4/1 protein interacts, both in yeast two-hybrid system and in vitro, and co-localizes in plant cells with plant BAP-like protein, the orthologue of human protein BAP31.
In yeast two-hybrid system, we identified a number of Nicotiana benthamiana protein interactors of Nt-4/1, the protein known to affect systemic transport of potato spindle tuber viroid. For one of these interactors, an orthologue of human B-cell receptor-associated protein 31 (BAP31) termed plant BAP-like protein (PBL), the ability to interact with Nt-4/1 was studied in greater detail. Analyses of purified proteins expressed in bacterial cells carried out in vitro with the surface plasmon resonance (SPR) spectroscopy revealed that the N. tabacum PBL (NtPBL) was able to interact with Nt-4/1 with high-affinity, and that their complex can form at physiologically relevant concentrations of both proteins. Subcellular localization studies of 4/1-GFP and NtPBL-mRFP transiently co-expressed in plant cells revealed the co-localization of the two fusion proteins in endoplasmic reticulum-associated bodies, suggesting their interaction in vivo. The N-terminal region of the Nt-4/1 protein was found to be required for the specific subcellular targeting of the protein, presumably due to a predicted amphipathic helix mediating association of the Nt-4/1 protein with cell membranes. Additionally, this region was found to contain a trans-activator domain responsible for the Nt-4/1 ability to activate transcription of a reporter gene in yeast.
Citations by journals
|
1
2
|
|
|
Biochimie
|
Biochimie
2 publications, 22.22%
|
|
Frontiers in Plant Science
|
Frontiers in Plant Science
1 publication, 11.11%
|
|
Plant Science
|
Plant Science
1 publication, 11.11%
|
|
Pharmacological Research
|
Pharmacological Research
1 publication, 11.11%
|
|
Proteomics
|
Proteomics
1 publication, 11.11%
|
|
Biochemistry (Moscow)
|
Biochemistry (Moscow)
1 publication, 11.11%
|
|
Journal of Experimental Botany
|
Journal of Experimental Botany
1 publication, 11.11%
|
|
1
2
|
Citations by publishers
|
1
2
3
4
|
|
|
Elsevier
|
Elsevier
4 publications, 44.44%
|
|
Frontiers Media S.A.
|
Frontiers Media S.A.
1 publication, 11.11%
|
|
Wiley
|
Wiley
1 publication, 11.11%
|
|
Pleiades Publishing
|
Pleiades Publishing
1 publication, 11.11%
|
|
Oxford University Press
|
Oxford University Press
1 publication, 11.11%
|
|
Cold Spring Harbor Laboratory
|
Cold Spring Harbor Laboratory
1 publication, 11.11%
|
|
1
2
3
4
|
- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
{"yearsCitations":{"type":"bar","data":{"show":true,"labels":[2017,2018,2019,2020,2021,2022,2023],"ids":[0,0,0,0,0,0,0],"codes":[0,0,0,0,0,0,0],"imageUrls":["","","","","","",""],"datasets":[{"label":"Citations number","data":[1,2,1,2,0,2,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":["11.11","22.22","11.11","22.22",0,"22.22","11.11"],"barThickness":null}]},"options":{"indexAxis":"x","maintainAspectRatio":true,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"}},"x":{"ticks":{"stepSize":1,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"}}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Citations per year","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}},"journals":{"type":"bar","data":{"show":true,"labels":["Biochimie","Frontiers in Plant Science","Plant Science","Pharmacological Research","Proteomics","Biochemistry (Moscow)","Journal of Experimental Botany"],"ids":[4794,1823,13422,4321,12149,2119,24056],"codes":[0,0,0,0,0,0,0],"imageUrls":["\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/4QWA67eqfcfyOiA8Wk7YnqroHFqQbTsmDJUYTCTg_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/oZgeErrVFhuDksyqFURLvYS1wtVSBWczh001igGo_medium.webp","\/storage\/images\/resized\/yNSijlgQghQF53VZuyFLA30CKDe4j3HK74Vtpnxa_medium.webp"],"datasets":[{"label":"","data":[2,1,1,1,1,1,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":[22.22,11.11,11.11,11.11,11.11,11.11,11.11],"barThickness":13}]},"options":{"indexAxis":"y","maintainAspectRatio":false,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"}},"x":{"ticks":{"stepSize":null,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"}}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Journals","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}},"publishers":{"type":"bar","data":{"show":true,"labels":["Elsevier","Frontiers Media S.A.","Wiley","Pleiades Publishing","Oxford University Press","Cold Spring Harbor Laboratory"],"ids":[17,208,11,101,19,6909],"codes":[0,0,0,0,0,0],"imageUrls":["\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/4QWA67eqfcfyOiA8Wk7YnqroHFqQbTsmDJUYTCTg_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/oZgeErrVFhuDksyqFURLvYS1wtVSBWczh001igGo_medium.webp","\/storage\/images\/resized\/yNSijlgQghQF53VZuyFLA30CKDe4j3HK74Vtpnxa_medium.webp","\/storage\/images\/resized\/hg4jJjT8wVGtHstBCc0zk465Mg9pLx3G4odCDOqE_medium.webp"],"datasets":[{"label":"","data":[4,1,1,1,1,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":[44.44,11.11,11.11,11.11,11.11,11.11],"barThickness":13}]},"options":{"indexAxis":"y","maintainAspectRatio":false,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"}},"x":{"ticks":{"stepSize":null,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"}}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Publishers","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}}}
Metrics
Cite this
GOST |
RIS |
BibTex |
MLA
Cite this
GOST
Copy
Pankratenko A. V. et al. Plant-specific 4/1 polypeptide interacts with an endoplasmic reticulum protein related to human BAP31 // Planta. 2016. Vol. 245. No. 1. pp. 193-205.
GOST all authors (up to 50)
Copy
Pankratenko A. V., Atabekova A. K., Lazareva E. A., Baksheeva V. E., Zhironkina O. A., Zernii E., Owens R. A., Solovyev A. G., Morozov S. Y. Plant-specific 4/1 polypeptide interacts with an endoplasmic reticulum protein related to human BAP31 // Planta. 2016. Vol. 245. No. 1. pp. 193-205.
Cite this
RIS
Copy
TY - JOUR
DO - 10.1007/s00425-016-2601-8
UR - https://doi.org/10.1007%2Fs00425-016-2601-8
TI - Plant-specific 4/1 polypeptide interacts with an endoplasmic reticulum protein related to human BAP31
T2 - Planta
AU - Pankratenko, Anna V
AU - Atabekova, Anastasia K
AU - Baksheeva, Viktoriia E.
AU - Zernii, Evgeni Yu.
AU - Zhironkina, Oxana A
AU - Owens, Robert A.
AU - Solovyev, Andrey G.
AU - Morozov, Sergey Y.
AU - Lazareva, Ekaterina A.
PY - 2016
DA - 2016/10/06 00:00:00
PB - Springer Nature
SP - 193-205
IS - 1
VL - 245
SN - 0032-0935
SN - 1432-2048
ER -
Cite this
BibTex
Copy
@article{2016_Pankratenko,
author = {Anna V Pankratenko and Anastasia K Atabekova and Viktoriia E. Baksheeva and Evgeni Yu. Zernii and Oxana A Zhironkina and Robert A. Owens and Andrey G. Solovyev and Sergey Y. Morozov and Ekaterina A. Lazareva},
title = {Plant-specific 4/1 polypeptide interacts with an endoplasmic reticulum protein related to human BAP31},
journal = {Planta},
year = {2016},
volume = {245},
publisher = {Springer Nature},
month = {oct},
url = {https://doi.org/10.1007%2Fs00425-016-2601-8},
number = {1},
pages = {193--205},
doi = {10.1007/s00425-016-2601-8}
}
Cite this
MLA
Copy
Pankratenko, Anna V., et al. “Plant-specific 4/1 polypeptide interacts with an endoplasmic reticulum protein related to human BAP31.” Planta, vol. 245, no. 1, Oct. 2016, pp. 193-205. https://doi.org/10.1007%2Fs00425-016-2601-8.
Profiles