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

• Autorzy: Ayaydin F. , Biro J. , Domoki M. , Ferenc G. , Feher A.
• Języki publikacji: EN

Abstrakty

EN

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-offunction 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.

• Wydawca: -
• Czasopismo: Acta Physiologiae Plantarum
• Rocznik: 2015
• Tom: 37
• Numer: 02
• Opis fizyczny: Article: 3 [8 p.], fig.,ref.

Twórcy

autor

Ayaydin F.

• Biological Research Center, Institute of Plant Biology, Hungarian Academy of Sciences, Temesvari krt. 62, PO Box 521, 6701 Szeged, Hungary

autor

Biro J.

• Biological Research Center, Institute of Plant Biology, Hungarian Academy of Sciences, Temesvari krt. 62, PO Box 521, 6701 Szeged, Hungary

autor

Domoki M.

• Biological Research Center, Institute of Plant Biology, Hungarian Academy of Sciences, Temesvari krt. 62, PO Box 521, 6701 Szeged, Hungary

autor

Ferenc G.

• Biological Research Center, Institute of Plant Biology, Hungarian Academy of Sciences, Temesvari krt. 62, PO Box 521, 6701 Szeged, Hungary

autor

Feher A.

• Biological Research Center, Institute of Plant Biology, Hungarian Academy of Sciences, Temesvari krt. 62, PO Box 521, 6701 Szeged, Hungary

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Identyfikatory

DOI

10.1007/s11738-014-1753-z