Functional Crypto-Adenylate Cyclases Operate in Complex Plant Proteins
Adenylyl cyclases (ACs) and their catalytic product cAMP are regulatory components of many plant responses. Here, we show that an amino acid search motif based on annotated adenylate cyclases (ACs) identifies 12 unique Arabidopsis thaliana candidate ACs, four of which have a role in the biosynthesis...
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2021-08-01
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doaj-e6e1bb1f7def492cb5de0495bf20cf7a2021-08-12T04:52:26ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2021-08-011210.3389/fpls.2021.711749711749Functional Crypto-Adenylate Cyclases Operate in Complex Plant ProteinsInas Al-Younis0Basem Moosa1Mateusz Kwiatkowski2Krzysztof Jaworski3Aloysius Wong4Aloysius Wong5Chris Gehring6Chris Gehring7Biological and Environmental Sciences and Engineering Division, King Abdullah University of Science and Technology, Thuwal, Saudi ArabiaPhysical Science and Engineering Division, King Abdullah University of Science and Technology, Thuwal, Saudi ArabiaChair of Plant Physiology and Biotechnology, Faculty of Biological and Veterinary Sciences, Nicolaus Copernicus University in Toruń, Toruń, PolandChair of Plant Physiology and Biotechnology, Faculty of Biological and Veterinary Sciences, Nicolaus Copernicus University in Toruń, Toruń, PolandDepartment of Biology, College of Science and Technology, Wenzhou-Kean University, Wenzhou, ChinaZhejiang Bioinformatics International Science and Technology Cooperation Center of Wenzhou-Kean University, Wenzhou, ChinaBiological and Environmental Sciences and Engineering Division, King Abdullah University of Science and Technology, Thuwal, Saudi ArabiaDepartment of Chemistry, Biology & Biotechnology, University of Perugia, Perugia, ItalyAdenylyl cyclases (ACs) and their catalytic product cAMP are regulatory components of many plant responses. Here, we show that an amino acid search motif based on annotated adenylate cyclases (ACs) identifies 12 unique Arabidopsis thaliana candidate ACs, four of which have a role in the biosynthesis of the stress hormone abscisic acid (ABA). One of these, the 9-cis-epoxycarotenoid dioxygenase (NCED3 and At3g14440), was identified by sequence and structural analysis as a putative AC and then tested experimentally with two different methods. Given that the in vitro activity is low (fmoles cAMP pmol−1 protein min−1), but highly reproducible, we term the enzyme a crypto-AC. Our results are consistent with a role for ACs with low activities in multi-domain moonlighting proteins that have at least one other distinct molecular function, such as catalysis or ion channel activation. We propose that crypto-ACs be examined from the perspective that considers their low activities as an innate feature of regulatory ACs embedded within multi-domain moonlighting proteins. It is therefore conceivable that crypto-ACs form integral components of complex plant proteins participating in intra-molecular regulatory mechanisms, and in this case, potentially linking cAMP to ABA synthesis.https://www.frontiersin.org/articles/10.3389/fpls.2021.711749/fulladenylyl cyclase3',5'-cyclic adenosine monophosphatecrypto-enzymesmulti-domain moonlighting enzymescatalytic centerArabidopsis thaliana |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Inas Al-Younis Basem Moosa Mateusz Kwiatkowski Krzysztof Jaworski Aloysius Wong Aloysius Wong Chris Gehring Chris Gehring |
spellingShingle |
Inas Al-Younis Basem Moosa Mateusz Kwiatkowski Krzysztof Jaworski Aloysius Wong Aloysius Wong Chris Gehring Chris Gehring Functional Crypto-Adenylate Cyclases Operate in Complex Plant Proteins Frontiers in Plant Science adenylyl cyclase 3',5'-cyclic adenosine monophosphate crypto-enzymes multi-domain moonlighting enzymes catalytic center Arabidopsis thaliana |
author_facet |
Inas Al-Younis Basem Moosa Mateusz Kwiatkowski Krzysztof Jaworski Aloysius Wong Aloysius Wong Chris Gehring Chris Gehring |
author_sort |
Inas Al-Younis |
title |
Functional Crypto-Adenylate Cyclases Operate in Complex Plant Proteins |
title_short |
Functional Crypto-Adenylate Cyclases Operate in Complex Plant Proteins |
title_full |
Functional Crypto-Adenylate Cyclases Operate in Complex Plant Proteins |
title_fullStr |
Functional Crypto-Adenylate Cyclases Operate in Complex Plant Proteins |
title_full_unstemmed |
Functional Crypto-Adenylate Cyclases Operate in Complex Plant Proteins |
title_sort |
functional crypto-adenylate cyclases operate in complex plant proteins |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Plant Science |
issn |
1664-462X |
publishDate |
2021-08-01 |
description |
Adenylyl cyclases (ACs) and their catalytic product cAMP are regulatory components of many plant responses. Here, we show that an amino acid search motif based on annotated adenylate cyclases (ACs) identifies 12 unique Arabidopsis thaliana candidate ACs, four of which have a role in the biosynthesis of the stress hormone abscisic acid (ABA). One of these, the 9-cis-epoxycarotenoid dioxygenase (NCED3 and At3g14440), was identified by sequence and structural analysis as a putative AC and then tested experimentally with two different methods. Given that the in vitro activity is low (fmoles cAMP pmol−1 protein min−1), but highly reproducible, we term the enzyme a crypto-AC. Our results are consistent with a role for ACs with low activities in multi-domain moonlighting proteins that have at least one other distinct molecular function, such as catalysis or ion channel activation. We propose that crypto-ACs be examined from the perspective that considers their low activities as an innate feature of regulatory ACs embedded within multi-domain moonlighting proteins. It is therefore conceivable that crypto-ACs form integral components of complex plant proteins participating in intra-molecular regulatory mechanisms, and in this case, potentially linking cAMP to ABA synthesis. |
topic |
adenylyl cyclase 3',5'-cyclic adenosine monophosphate crypto-enzymes multi-domain moonlighting enzymes catalytic center Arabidopsis thaliana |
url |
https://www.frontiersin.org/articles/10.3389/fpls.2021.711749/full |
work_keys_str_mv |
AT inasalyounis functionalcryptoadenylatecyclasesoperateincomplexplantproteins AT basemmoosa functionalcryptoadenylatecyclasesoperateincomplexplantproteins AT mateuszkwiatkowski functionalcryptoadenylatecyclasesoperateincomplexplantproteins AT krzysztofjaworski functionalcryptoadenylatecyclasesoperateincomplexplantproteins AT aloysiuswong functionalcryptoadenylatecyclasesoperateincomplexplantproteins AT aloysiuswong functionalcryptoadenylatecyclasesoperateincomplexplantproteins AT chrisgehring functionalcryptoadenylatecyclasesoperateincomplexplantproteins AT chrisgehring functionalcryptoadenylatecyclasesoperateincomplexplantproteins |
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