Identification of interacting proteins of Arabidopsis cyclophilin38 (AtCYP38) via multiple screening approaches reveals its possible broad functions in chloroplasts

Copyright © 2021. Published by Elsevier GmbH.

Bibliographische Detailangaben
Veröffentlicht in:Journal of plant physiology. - 1979. - 264(2021) vom: 15. Sept., Seite 153487
1. Verfasser: Hao, Yaqi (VerfasserIn)
Weitere Verfasser: Chu, Jiashu, Shi, Lujing, Ma, Cong, Hui, Liangliang, Cao, Xiaofei, Wang, Yuhua, Xu, Min, Fu, Aigen
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2021
Zugriff auf das übergeordnete Werk:Journal of plant physiology
Schlagworte:Journal Article AtCYP38 Chloroplast thylakoid lumen Interacting proteins Yeast two-hybrid Arabidopsis Proteins Photosystem II Protein Complex Cyclophilins EC 5.2.1.- cyclophilin 38, Arabidopsis
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520 |a AtCYP38, a thylakoid lumen localized immunophilin, is found to be essential for photosystem II assembly and maintenance, but how AtCYP38 functions in chloroplast remains unknown. Based on previous functional studies and its crystal structure, we hypothesize that AtCYP38 should function via binding its targets or cofactors in the thylakoid lumen. To identify potential interacting proteins of AtCYP38, we first adopted ATTED-II and STRING web-tools, and found 12 proteins functionally related to AtCYP38. We then screened a yeast two-hybrid library including an Arabidopsis genome wide cDNA with different domain of AtCYP38, and five thylakoid lumen-localized targets were identified. In order to specifically search interacting proteins of AtCYP38 in the thylakoid lumen, we generated a yeast two-hybrid mini library including the thylakoid lumenal proteins and lumenal fractions of thylakoid membrane proteins, and we obtained six thylakoid membrane proteins and nine thylakoid lumenal proteins as interacting proteins of AtCYP38. The interactions between AtCYP38 and several potential targets were further confirmed via pull-down and co-immunoprecipitation assays. Together, a couple of new potential candidate interacting proteins of AtCYP38 were identified, and the results will lay a foundation for unveiling the regulatory mechanisms in photosynthesis by AtCYP38 
650 4 |a Journal Article 
650 4 |a AtCYP38 
650 4 |a Chloroplast thylakoid lumen 
650 4 |a Interacting proteins 
650 4 |a Yeast two-hybrid 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Photosystem II Protein Complex  |2 NLM 
650 7 |a Cyclophilins  |2 NLM 
650 7 |a EC 5.2.1.-  |2 NLM 
650 7 |a cyclophilin 38, Arabidopsis  |2 NLM 
650 7 |a EC 5.2.1.-  |2 NLM 
700 1 |a Chu, Jiashu  |e verfasserin  |4 aut 
700 1 |a Shi, Lujing  |e verfasserin  |4 aut 
700 1 |a Ma, Cong  |e verfasserin  |4 aut 
700 1 |a Hui, Liangliang  |e verfasserin  |4 aut 
700 1 |a Cao, Xiaofei  |e verfasserin  |4 aut 
700 1 |a Wang, Yuhua  |e verfasserin  |4 aut 
700 1 |a Xu, Min  |e verfasserin  |4 aut 
700 1 |a Fu, Aigen  |e verfasserin  |4 aut 
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