Regulation of abiotic stress signalling by arabidopsis C-terminal domain phosphatase-like 1 requires interaction with a K-homology domain-containing protein

In Sil Jeong, Akihito Fukudome, Emre Aksoy, Woo Young Bang, Sewon Kim, Qingmei Guan, Jeong Dong Bahk, Kimberly A. May, William Russell, Jianhua Zhu, Hisashi Koiwa

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Arabidopsis thaliana CARBOXYL-TERMINAL DOMAIN (CTD) PHOSPHATASE-LIKE 1 (CPL1) regulates plant transcriptional responses to diverse stress signals. Unlike typical CTD phosphatases, CPL1 contains two double-stranded (ds) RNA binding motifs (dsRBMs) at its C-terminus. Some dsRBMs can bind to dsRNA and/or other proteins, but the function of the CPL1 dsRBMs has remained obscure. Here, we report identification of REGULATOR OF CBF GENE EXPRESSION 3 (RCF3) as a CPL1-interacting protein. RCF3 co-purified with tandem-affinity-tagged CPL1 from cultured Arabidopsis cells and contains multiple K-homology (KH) domains, which were predicted to be important for binding to single-stranded DNA/RNA. Yeast two-hybrid, luciferase complementation imaging, and bimolecular fluorescence complementation analyses established that CPL1 and RCF3 strongly associate in vivo, an interaction mediated by the dsRBM1 of CPL1 and the KH3/KH4 domains of RCF3. Mapping of functional regions of CPL1 indicated that CPL1 in vivo function requires the dsRBM1, catalytic activity, and nuclear targeting of CPL1. Gene expression profiles of rcf3 and cpl1 mutants were similar during iron deficiency, but were distinct during the cold response. These results suggest that tethering CPL1 to RCF3 via dsRBM1 is part of the mechanism that confers specificity to CPL1-mediated transcriptional regulation.

Original languageEnglish (US)
Article numbere80509
JournalPLoS One
Volume8
Issue number11
DOIs
StatePublished - Nov 26 2013
Externally publishedYes

Fingerprint

sequence homology
Phosphoric Monoester Hydrolases
Arabidopsis
abiotic stress
regulator genes
gene expression
Gene expression
Regulator Genes
Proteins
proteins
double-stranded RNA
RNA
Gene Expression
single-stranded DNA
luciferase
catalytic activity
Protein Domains
carboxy-terminal domain phosphatase
stress response
Arabidopsis thaliana

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

Regulation of abiotic stress signalling by arabidopsis C-terminal domain phosphatase-like 1 requires interaction with a K-homology domain-containing protein. / Jeong, In Sil; Fukudome, Akihito; Aksoy, Emre; Bang, Woo Young; Kim, Sewon; Guan, Qingmei; Bahk, Jeong Dong; May, Kimberly A.; Russell, William; Zhu, Jianhua; Koiwa, Hisashi.

In: PLoS One, Vol. 8, No. 11, e80509, 26.11.2013.

Research output: Contribution to journalArticle

Jeong, In Sil ; Fukudome, Akihito ; Aksoy, Emre ; Bang, Woo Young ; Kim, Sewon ; Guan, Qingmei ; Bahk, Jeong Dong ; May, Kimberly A. ; Russell, William ; Zhu, Jianhua ; Koiwa, Hisashi. / Regulation of abiotic stress signalling by arabidopsis C-terminal domain phosphatase-like 1 requires interaction with a K-homology domain-containing protein. In: PLoS One. 2013 ; Vol. 8, No. 11.
@article{c5640113406d44bdac7e30a518337c29,
title = "Regulation of abiotic stress signalling by arabidopsis C-terminal domain phosphatase-like 1 requires interaction with a K-homology domain-containing protein",
abstract = "Arabidopsis thaliana CARBOXYL-TERMINAL DOMAIN (CTD) PHOSPHATASE-LIKE 1 (CPL1) regulates plant transcriptional responses to diverse stress signals. Unlike typical CTD phosphatases, CPL1 contains two double-stranded (ds) RNA binding motifs (dsRBMs) at its C-terminus. Some dsRBMs can bind to dsRNA and/or other proteins, but the function of the CPL1 dsRBMs has remained obscure. Here, we report identification of REGULATOR OF CBF GENE EXPRESSION 3 (RCF3) as a CPL1-interacting protein. RCF3 co-purified with tandem-affinity-tagged CPL1 from cultured Arabidopsis cells and contains multiple K-homology (KH) domains, which were predicted to be important for binding to single-stranded DNA/RNA. Yeast two-hybrid, luciferase complementation imaging, and bimolecular fluorescence complementation analyses established that CPL1 and RCF3 strongly associate in vivo, an interaction mediated by the dsRBM1 of CPL1 and the KH3/KH4 domains of RCF3. Mapping of functional regions of CPL1 indicated that CPL1 in vivo function requires the dsRBM1, catalytic activity, and nuclear targeting of CPL1. Gene expression profiles of rcf3 and cpl1 mutants were similar during iron deficiency, but were distinct during the cold response. These results suggest that tethering CPL1 to RCF3 via dsRBM1 is part of the mechanism that confers specificity to CPL1-mediated transcriptional regulation.",
author = "Jeong, {In Sil} and Akihito Fukudome and Emre Aksoy and Bang, {Woo Young} and Sewon Kim and Qingmei Guan and Bahk, {Jeong Dong} and May, {Kimberly A.} and William Russell and Jianhua Zhu and Hisashi Koiwa",
year = "2013",
month = "11",
day = "26",
doi = "10.1371/journal.pone.0080509",
language = "English (US)",
volume = "8",
journal = "PLoS One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "11",

}

TY - JOUR

T1 - Regulation of abiotic stress signalling by arabidopsis C-terminal domain phosphatase-like 1 requires interaction with a K-homology domain-containing protein

AU - Jeong, In Sil

AU - Fukudome, Akihito

AU - Aksoy, Emre

AU - Bang, Woo Young

AU - Kim, Sewon

AU - Guan, Qingmei

AU - Bahk, Jeong Dong

AU - May, Kimberly A.

AU - Russell, William

AU - Zhu, Jianhua

AU - Koiwa, Hisashi

PY - 2013/11/26

Y1 - 2013/11/26

N2 - Arabidopsis thaliana CARBOXYL-TERMINAL DOMAIN (CTD) PHOSPHATASE-LIKE 1 (CPL1) regulates plant transcriptional responses to diverse stress signals. Unlike typical CTD phosphatases, CPL1 contains two double-stranded (ds) RNA binding motifs (dsRBMs) at its C-terminus. Some dsRBMs can bind to dsRNA and/or other proteins, but the function of the CPL1 dsRBMs has remained obscure. Here, we report identification of REGULATOR OF CBF GENE EXPRESSION 3 (RCF3) as a CPL1-interacting protein. RCF3 co-purified with tandem-affinity-tagged CPL1 from cultured Arabidopsis cells and contains multiple K-homology (KH) domains, which were predicted to be important for binding to single-stranded DNA/RNA. Yeast two-hybrid, luciferase complementation imaging, and bimolecular fluorescence complementation analyses established that CPL1 and RCF3 strongly associate in vivo, an interaction mediated by the dsRBM1 of CPL1 and the KH3/KH4 domains of RCF3. Mapping of functional regions of CPL1 indicated that CPL1 in vivo function requires the dsRBM1, catalytic activity, and nuclear targeting of CPL1. Gene expression profiles of rcf3 and cpl1 mutants were similar during iron deficiency, but were distinct during the cold response. These results suggest that tethering CPL1 to RCF3 via dsRBM1 is part of the mechanism that confers specificity to CPL1-mediated transcriptional regulation.

AB - Arabidopsis thaliana CARBOXYL-TERMINAL DOMAIN (CTD) PHOSPHATASE-LIKE 1 (CPL1) regulates plant transcriptional responses to diverse stress signals. Unlike typical CTD phosphatases, CPL1 contains two double-stranded (ds) RNA binding motifs (dsRBMs) at its C-terminus. Some dsRBMs can bind to dsRNA and/or other proteins, but the function of the CPL1 dsRBMs has remained obscure. Here, we report identification of REGULATOR OF CBF GENE EXPRESSION 3 (RCF3) as a CPL1-interacting protein. RCF3 co-purified with tandem-affinity-tagged CPL1 from cultured Arabidopsis cells and contains multiple K-homology (KH) domains, which were predicted to be important for binding to single-stranded DNA/RNA. Yeast two-hybrid, luciferase complementation imaging, and bimolecular fluorescence complementation analyses established that CPL1 and RCF3 strongly associate in vivo, an interaction mediated by the dsRBM1 of CPL1 and the KH3/KH4 domains of RCF3. Mapping of functional regions of CPL1 indicated that CPL1 in vivo function requires the dsRBM1, catalytic activity, and nuclear targeting of CPL1. Gene expression profiles of rcf3 and cpl1 mutants were similar during iron deficiency, but were distinct during the cold response. These results suggest that tethering CPL1 to RCF3 via dsRBM1 is part of the mechanism that confers specificity to CPL1-mediated transcriptional regulation.

UR - http://www.scopus.com/inward/record.url?scp=84896709256&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84896709256&partnerID=8YFLogxK

U2 - 10.1371/journal.pone.0080509

DO - 10.1371/journal.pone.0080509

M3 - Article

VL - 8

JO - PLoS One

JF - PLoS One

SN - 1932-6203

IS - 11

M1 - e80509

ER -