Arabidopsis NAP-related proteins (NRPs) are soluble nuclear proteins immobilized by heat

F. Ayaydin, Judit Bíró, Mónika Domoki, Györgyi Ferenc, A. Fehér

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Nucleosome assembly protein-related proteins (NRPs) are multifunctional proteins having histone chaperone and phosphatase inhibitor properties. Although it is believed that these proteins are nuclear and bind the chromatin, they can be detected in the cytoplasmic but not in the nuclear protein fraction by immunoblotting analysis. It is shown here that under normal conditions, NRPs are nuclear but soluble and leak out of the nuclei during their purification. However, under elevated temperatures (above 42 °C), NRPs display significantly reduced mobility and are retained in the nuclei during purification probably due to binding other immobile macromolecules in the nucleus. Our observations highlight the necessity to use different techniques in parallel to unambiguously determine the intracellular localization of proteins. As heat adapted (38 °C, 2 h followed by 2 h recovery) and heat shocked (45 °C, 1 h), Arabidopsis seedlings were found to have phenotypes similar to those observed in the NRP loss-of-function mutants nrp1-1 nrp2-1 (short, branching roots, increased bleomycin sensitivity), it was also investigated whether the immobilization of NRPs by heat results in disturbed NRP functions. The results indicated, however, that heat affected the investigated traits independent on the presence of NRPs.

Original languageEnglish
JournalActa Physiologiae Plantarum
Volume37
Issue number2
DOIs
Publication statusPublished - 2015

Fingerprint

nuclear proteins
Nuclear Proteins
Hot Temperature
Arabidopsis
heat
Proteins
proteins
Histone Chaperones
Arabidopsis NAP protein
Nucleosomes
Bleomycin
nucleosomes
protein depletion
Seedlings
Phosphoric Monoester Hydrolases
Immunoblotting
Immobilization
immunoblotting
Chromatin
histones

Keywords

  • Arabidopsis thaliana (L.)
  • Cellular localization
  • Heat shock
  • Nuclear protein
  • Nucleosome assembly protein-related protein
  • Protein mobility

ASJC Scopus subject areas

  • Plant Science
  • Physiology
  • Agronomy and Crop Science

Cite this

Arabidopsis NAP-related proteins (NRPs) are soluble nuclear proteins immobilized by heat. / Ayaydin, F.; Bíró, Judit; Domoki, Mónika; Ferenc, Györgyi; Fehér, A.

In: Acta Physiologiae Plantarum, Vol. 37, No. 2, 2015.

Research output: Contribution to journalArticle

@article{760fce68dfd14e318caad121e0b0e245,
title = "Arabidopsis NAP-related proteins (NRPs) are soluble nuclear proteins immobilized by heat",
abstract = "Nucleosome assembly protein-related proteins (NRPs) are multifunctional proteins having histone chaperone and phosphatase inhibitor properties. Although it is believed that these proteins are nuclear and bind the chromatin, they can be detected in the cytoplasmic but not in the nuclear protein fraction by immunoblotting analysis. It is shown here that under normal conditions, NRPs are nuclear but soluble and leak out of the nuclei during their purification. However, under elevated temperatures (above 42 °C), NRPs display significantly reduced mobility and are retained in the nuclei during purification probably due to binding other immobile macromolecules in the nucleus. Our observations highlight the necessity to use different techniques in parallel to unambiguously determine the intracellular localization of proteins. As heat adapted (38 °C, 2 h followed by 2 h recovery) and heat shocked (45 °C, 1 h), Arabidopsis seedlings were found to have phenotypes similar to those observed in the NRP loss-of-function mutants nrp1-1 nrp2-1 (short, branching roots, increased bleomycin sensitivity), it was also investigated whether the immobilization of NRPs by heat results in disturbed NRP functions. The results indicated, however, that heat affected the investigated traits independent on the presence of NRPs.",
keywords = "Arabidopsis thaliana (L.), Cellular localization, Heat shock, Nuclear protein, Nucleosome assembly protein-related protein, Protein mobility",
author = "F. Ayaydin and Judit B{\'i}r{\'o} and M{\'o}nika Domoki and Gy{\"o}rgyi Ferenc and A. Feh{\'e}r",
year = "2015",
doi = "10.1007/s11738-014-1753-z",
language = "English",
volume = "37",
journal = "Acta Physiologiae Plantarum",
issn = "0137-5881",
publisher = "Polish Academy of Sciences Publishing House",
number = "2",

}

TY - JOUR

T1 - Arabidopsis NAP-related proteins (NRPs) are soluble nuclear proteins immobilized by heat

AU - Ayaydin, F.

AU - Bíró, Judit

AU - Domoki, Mónika

AU - Ferenc, Györgyi

AU - Fehér, A.

PY - 2015

Y1 - 2015

N2 - Nucleosome assembly protein-related proteins (NRPs) are multifunctional proteins having histone chaperone and phosphatase inhibitor properties. Although it is believed that these proteins are nuclear and bind the chromatin, they can be detected in the cytoplasmic but not in the nuclear protein fraction by immunoblotting analysis. It is shown here that under normal conditions, NRPs are nuclear but soluble and leak out of the nuclei during their purification. However, under elevated temperatures (above 42 °C), NRPs display significantly reduced mobility and are retained in the nuclei during purification probably due to binding other immobile macromolecules in the nucleus. Our observations highlight the necessity to use different techniques in parallel to unambiguously determine the intracellular localization of proteins. As heat adapted (38 °C, 2 h followed by 2 h recovery) and heat shocked (45 °C, 1 h), Arabidopsis seedlings were found to have phenotypes similar to those observed in the NRP loss-of-function mutants nrp1-1 nrp2-1 (short, branching roots, increased bleomycin sensitivity), it was also investigated whether the immobilization of NRPs by heat results in disturbed NRP functions. The results indicated, however, that heat affected the investigated traits independent on the presence of NRPs.

AB - Nucleosome assembly protein-related proteins (NRPs) are multifunctional proteins having histone chaperone and phosphatase inhibitor properties. Although it is believed that these proteins are nuclear and bind the chromatin, they can be detected in the cytoplasmic but not in the nuclear protein fraction by immunoblotting analysis. It is shown here that under normal conditions, NRPs are nuclear but soluble and leak out of the nuclei during their purification. However, under elevated temperatures (above 42 °C), NRPs display significantly reduced mobility and are retained in the nuclei during purification probably due to binding other immobile macromolecules in the nucleus. Our observations highlight the necessity to use different techniques in parallel to unambiguously determine the intracellular localization of proteins. As heat adapted (38 °C, 2 h followed by 2 h recovery) and heat shocked (45 °C, 1 h), Arabidopsis seedlings were found to have phenotypes similar to those observed in the NRP loss-of-function mutants nrp1-1 nrp2-1 (short, branching roots, increased bleomycin sensitivity), it was also investigated whether the immobilization of NRPs by heat results in disturbed NRP functions. The results indicated, however, that heat affected the investigated traits independent on the presence of NRPs.

KW - Arabidopsis thaliana (L.)

KW - Cellular localization

KW - Heat shock

KW - Nuclear protein

KW - Nucleosome assembly protein-related protein

KW - Protein mobility

UR - http://www.scopus.com/inward/record.url?scp=84921897741&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84921897741&partnerID=8YFLogxK

U2 - 10.1007/s11738-014-1753-z

DO - 10.1007/s11738-014-1753-z

M3 - Article

VL - 37

JO - Acta Physiologiae Plantarum

JF - Acta Physiologiae Plantarum

SN - 0137-5881

IS - 2

ER -