Plant 4/1 protein: potential player in intracellular, cell-to-cell and long-distance signaling

Originally isolated as a result of its ability to interact with the movement protein of Tomato spotted wilt virus in a yeast two-hybrid system, the 4/1 protein is proving to be an excellent tool for studying intracellular protein trafficking and intercellular communication. Expression of 4/1 in vivo...

Full description

Bibliographic Details
Main Authors: Sergey eMorozov, Svetlana eMakarova, Tatyana eErokhina, Lilya eKopertekh, Joachim eSchiemann, Robert eOwens, Andrey eSolovyev
Format: Article
Language:English
Published: Frontiers Media S.A. 2014-02-01
Series:Frontiers in Plant Science
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fpls.2014.00026/full
_version_ 1818539110942375936
author Sergey eMorozov
Svetlana eMakarova
Tatyana eErokhina
Lilya eKopertekh
Joachim eSchiemann
Robert eOwens
Andrey eSolovyev
author_facet Sergey eMorozov
Svetlana eMakarova
Tatyana eErokhina
Lilya eKopertekh
Joachim eSchiemann
Robert eOwens
Andrey eSolovyev
author_sort Sergey eMorozov
collection DOAJ
description Originally isolated as a result of its ability to interact with the movement protein of Tomato spotted wilt virus in a yeast two-hybrid system, the 4/1 protein is proving to be an excellent tool for studying intracellular protein trafficking and intercellular communication. Expression of 4/1 in vivo is tightly regulated, first appearing in the veins of the cotyledon and later in the vasculature of the leaf and stem in association with the xylem parenchyma and phloem parenchyma. Structural studies indicate that 4/1 proteins contain as many as 5 coiled-coil (CC) domains; indeed, the highest level of sequence identity among 4/1 proteins involves their C-terminal CC domains, suggesting that protein-protein interaction is important for biological function. Recent data predict that the tertiary structure of this C-terminal CC domain is strikingly similar to that of yeast protein She2p; furthermore, like She2p, 4/1 protein exhibits RNA-binding activity, and mutational analysis has shown that the C-terminal CC domain is responsible for RNA binding. The 4/1 protein contains a nuclear export signal. Additional microscopy studies involving leptomycin and computer prediction suggest the presence of a nuclear localization signal as well.
first_indexed 2024-12-11T21:37:44Z
format Article
id doaj.art-70ddf0aa868b4ee09c658bdc23c0f8c9
institution Directory Open Access Journal
issn 1664-462X
language English
last_indexed 2024-12-11T21:37:44Z
publishDate 2014-02-01
publisher Frontiers Media S.A.
record_format Article
series Frontiers in Plant Science
spelling doaj.art-70ddf0aa868b4ee09c658bdc23c0f8c92022-12-22T00:49:58ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2014-02-01510.3389/fpls.2014.0002678295Plant 4/1 protein: potential player in intracellular, cell-to-cell and long-distance signalingSergey eMorozov0Svetlana eMakarova1Tatyana eErokhina2Lilya eKopertekh3Joachim eSchiemann4Robert eOwens5Andrey eSolovyev6Moscow State UniversityBiological Faculty, Moscow State UniversityRussian Academy of SciencesJulius Kühn InstituteJulius Kühn InstituteUSDA/ARSMoscow State UniversityOriginally isolated as a result of its ability to interact with the movement protein of Tomato spotted wilt virus in a yeast two-hybrid system, the 4/1 protein is proving to be an excellent tool for studying intracellular protein trafficking and intercellular communication. Expression of 4/1 in vivo is tightly regulated, first appearing in the veins of the cotyledon and later in the vasculature of the leaf and stem in association with the xylem parenchyma and phloem parenchyma. Structural studies indicate that 4/1 proteins contain as many as 5 coiled-coil (CC) domains; indeed, the highest level of sequence identity among 4/1 proteins involves their C-terminal CC domains, suggesting that protein-protein interaction is important for biological function. Recent data predict that the tertiary structure of this C-terminal CC domain is strikingly similar to that of yeast protein She2p; furthermore, like She2p, 4/1 protein exhibits RNA-binding activity, and mutational analysis has shown that the C-terminal CC domain is responsible for RNA binding. The 4/1 protein contains a nuclear export signal. Additional microscopy studies involving leptomycin and computer prediction suggest the presence of a nuclear localization signal as well.http://journal.frontiersin.org/Journal/10.3389/fpls.2014.00026/fullPhloem transportRNA binding proteinIntracellular transportLong-distance signalingcell-to-cell transport
spellingShingle Sergey eMorozov
Svetlana eMakarova
Tatyana eErokhina
Lilya eKopertekh
Joachim eSchiemann
Robert eOwens
Andrey eSolovyev
Plant 4/1 protein: potential player in intracellular, cell-to-cell and long-distance signaling
Frontiers in Plant Science
Phloem transport
RNA binding protein
Intracellular transport
Long-distance signaling
cell-to-cell transport
title Plant 4/1 protein: potential player in intracellular, cell-to-cell and long-distance signaling
title_full Plant 4/1 protein: potential player in intracellular, cell-to-cell and long-distance signaling
title_fullStr Plant 4/1 protein: potential player in intracellular, cell-to-cell and long-distance signaling
title_full_unstemmed Plant 4/1 protein: potential player in intracellular, cell-to-cell and long-distance signaling
title_short Plant 4/1 protein: potential player in intracellular, cell-to-cell and long-distance signaling
title_sort plant 4 1 protein potential player in intracellular cell to cell and long distance signaling
topic Phloem transport
RNA binding protein
Intracellular transport
Long-distance signaling
cell-to-cell transport
url http://journal.frontiersin.org/Journal/10.3389/fpls.2014.00026/full
work_keys_str_mv AT sergeyemorozov plant41proteinpotentialplayerinintracellularcelltocellandlongdistancesignaling
AT svetlanaemakarova plant41proteinpotentialplayerinintracellularcelltocellandlongdistancesignaling
AT tatyanaeerokhina plant41proteinpotentialplayerinintracellularcelltocellandlongdistancesignaling
AT lilyaekopertekh plant41proteinpotentialplayerinintracellularcelltocellandlongdistancesignaling
AT joachimeschiemann plant41proteinpotentialplayerinintracellularcelltocellandlongdistancesignaling
AT roberteowens plant41proteinpotentialplayerinintracellularcelltocellandlongdistancesignaling
AT andreyesolovyev plant41proteinpotentialplayerinintracellularcelltocellandlongdistancesignaling