A low molecular-weight cyclophilin localizes in different cell compartments of Pyrus communis pollen and is released in vitro under Ca2+ depletion

Copyright © 2019 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 144(2019) vom: 15. Nov., Seite 197-206
1. Verfasser: Parrotta, Luigi (VerfasserIn)
Weitere Verfasser: Aloisi, Iris, Suanno, Chiara, Faleri, Claudia, Kiełbowicz-Matuk, Agnieszka, Bini, Luca, Cai, Giampiero, Del Duca, Stefano
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Cyclophilin EGTA Pollen tube Pyrus communis Cyclophilins EC 5.2.1.- Calcium SY7Q814VUP
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245 1 2 |a A low molecular-weight cyclophilin localizes in different cell compartments of Pyrus communis pollen and is released in vitro under Ca2+ depletion 
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520 |a Copyright © 2019 Elsevier Masson SAS. All rights reserved. 
520 |a Cyclophilins (CyPs) are ubiquitous proteins involved in a wide variety of processes including protein maturation and trafficking, receptor complex stabilization, apoptosis, receptor signaling, RNA processing, and spliceosome assembly. The ubiquitous presence is justified by their peptidyl-prolyl cis-trans isomerase (PPIase) activity, catalyzing the rotation of X-Pro peptide bonds from a cis to a trans conformation, a critical rate-limiting step in protein folding, as over 90% of proteins contain trans prolyl imide bonds. In Arabidopsis 35 CyPs involved in plant development have been reported, showing different subcellular localizations and tissue- and stage-specific expression. In the present work, we focused on the localization of CyPs in pear (Pyrus communis) pollen, a model system for studies on pollen tube elongation and on pollen-pistil self-incompatibility response. Fluorescent, confocal and immuno-electron microscopy showed that this protein is present in the cytoplasm, organelles and cell wall, as confirmed by protein fractionation. Moreover, an 18-kDa CyP isoform was specifically released extracellularly when pear pollen was incubated with the Ca2+ chelator EGTA 
650 4 |a Journal Article 
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650 7 |a Calcium  |2 NLM 
650 7 |a SY7Q814VUP  |2 NLM 
700 1 |a Aloisi, Iris  |e verfasserin  |4 aut 
700 1 |a Suanno, Chiara  |e verfasserin  |4 aut 
700 1 |a Faleri, Claudia  |e verfasserin  |4 aut 
700 1 |a Kiełbowicz-Matuk, Agnieszka  |e verfasserin  |4 aut 
700 1 |a Bini, Luca  |e verfasserin  |4 aut 
700 1 |a Cai, Giampiero  |e verfasserin  |4 aut 
700 1 |a Del Duca, Stefano  |e verfasserin  |4 aut 
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773 1 8 |g volume:144  |g year:2019  |g day:15  |g month:11  |g pages:197-206 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2019.09.045  |3 Volltext 
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