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Article: Overlapping functions of the paralogous proteins AtPAP2 and AtPAP9 in Arabidopsis thaliana

TitleOverlapping functions of the paralogous proteins AtPAP2 and AtPAP9 in Arabidopsis thaliana
Authors
KeywordsAtPAP2
AtPAP9
chloroplasts
import
mitochondria
Issue Date2021
PublisherMolecular Diversity Preservation International. The Journal's web site is located at http://www.mdpi.org/ijms
Citation
International Journal of Molecular Sciences, 2021, v. 22 n. 14, p. article no. 7243 How to Cite?
AbstractArabidopsis thaliana purple acid phosphatase 2 (AtPAP2), which is anchored to the outer membranes of chloroplasts and mitochondria, affects carbon metabolism by modulating the import of some preproteins into chloroplasts and mitochondria. AtPAP9 bears a 72% amino acid sequence identity with AtPAP2, and both pro-teins carry a hydrophobic motif at their C-termini. Here, we show that AtPAP9 is a tail-anchored protein targeted to the outer membrane of chloroplasts. Yeast two-hybrid and bimolecular fluorescence complementation experiments demonstrated that both AtPAP9 and AtPAP2 bind to a small subunit of Rubisco 1B (AtSSU1B) and a number of chloroplast proteins. Chloroplast import assays using [35S]-labeled AtSSU1B showed that like AtPAP2, AtPAP9 also plays a role in AtSSU1B import into chloroplasts. Based on these data, we propose that AtPAP9 and AtPAP2 perform overlapping roles in modulating the import of specific proteins into chloroplasts. Most plant genomes contain only one PAP-like sequence encoding a protein with a hydrophobic motif at the C-terminus. The presence of both AtPAP2 and AtPAP9 in the Arabidopsis genome may have arisen from genome duplication in Brassicaceae. Unlike AtPAP2 overexpression lines, the AtPAP9 overexpression lines did not exhibit early-bolting or high-seed-yield phenotypes. Their differential growth phenotypes could be due to the inability of AtPAP9 to be targeted to mitochondria, as the overexpression of AtPAP2 on mitochondria enhances the capacity of mitochondria to consume reducing equivalents.
Persistent Identifierhttp://hdl.handle.net/10722/301345
ISSN
2011 Impact Factor: 2.598
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorZhang, R-
dc.contributor.authorGuan, X-
dc.contributor.authorYANG, M-
dc.contributor.authorLaw, YS-
dc.contributor.authorVoon, CP-
dc.contributor.authorYan, J-
dc.contributor.authorSun, F-
dc.contributor.authorLim, BL-
dc.date.accessioned2021-07-27T08:09:42Z-
dc.date.available2021-07-27T08:09:42Z-
dc.date.issued2021-
dc.identifier.citationInternational Journal of Molecular Sciences, 2021, v. 22 n. 14, p. article no. 7243-
dc.identifier.issn1661-6596-
dc.identifier.urihttp://hdl.handle.net/10722/301345-
dc.description.abstractArabidopsis thaliana purple acid phosphatase 2 (AtPAP2), which is anchored to the outer membranes of chloroplasts and mitochondria, affects carbon metabolism by modulating the import of some preproteins into chloroplasts and mitochondria. AtPAP9 bears a 72% amino acid sequence identity with AtPAP2, and both pro-teins carry a hydrophobic motif at their C-termini. Here, we show that AtPAP9 is a tail-anchored protein targeted to the outer membrane of chloroplasts. Yeast two-hybrid and bimolecular fluorescence complementation experiments demonstrated that both AtPAP9 and AtPAP2 bind to a small subunit of Rubisco 1B (AtSSU1B) and a number of chloroplast proteins. Chloroplast import assays using [35S]-labeled AtSSU1B showed that like AtPAP2, AtPAP9 also plays a role in AtSSU1B import into chloroplasts. Based on these data, we propose that AtPAP9 and AtPAP2 perform overlapping roles in modulating the import of specific proteins into chloroplasts. Most plant genomes contain only one PAP-like sequence encoding a protein with a hydrophobic motif at the C-terminus. The presence of both AtPAP2 and AtPAP9 in the Arabidopsis genome may have arisen from genome duplication in Brassicaceae. Unlike AtPAP2 overexpression lines, the AtPAP9 overexpression lines did not exhibit early-bolting or high-seed-yield phenotypes. Their differential growth phenotypes could be due to the inability of AtPAP9 to be targeted to mitochondria, as the overexpression of AtPAP2 on mitochondria enhances the capacity of mitochondria to consume reducing equivalents.-
dc.languageeng-
dc.publisherMolecular Diversity Preservation International. The Journal's web site is located at http://www.mdpi.org/ijms-
dc.relation.ispartofInternational Journal of Molecular Sciences-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectAtPAP2-
dc.subjectAtPAP9-
dc.subjectchloroplasts-
dc.subjectimport-
dc.subjectmitochondria-
dc.titleOverlapping functions of the paralogous proteins AtPAP2 and AtPAP9 in Arabidopsis thaliana-
dc.typeArticle-
dc.identifier.emailLim, BL: bllim@hku.hk-
dc.identifier.authorityLim, BL=rp00744-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.3390/ijms22147243-
dc.identifier.pmid34298863-
dc.identifier.pmcidPMC8303434-
dc.identifier.scopuseid_2-s2.0-85109109888-
dc.identifier.hkuros323525-
dc.identifier.volume22-
dc.identifier.issue14-
dc.identifier.spagearticle no. 7243-
dc.identifier.epagearticle no. 7243-
dc.publisher.placeSwitzerland-

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