Document Type
Article
Publication Date
11-10-2021
Publication Title
Science Advances
Publisher
American Association for the Advancement of Science
Publisher Location
Washington, D.C.
Volume
7
Issue
46
First page number:
1
Last page number:
14
Abstract
Ethylene plays profound roles in plant development. The rate-limiting enzyme of ethylene biosynthesis is 1-aminocyclopropane-1-carboxylate (ACC) synthase (ACS), which is generally believed to be a single-activity enzyme evolving from aspartate aminotransferases. Here, we demonstrate that, in addition to catalyzing the conversion of S-adenosyl-methionine to the ethylene precursor ACC, genuine ACSs widely have Cβ-S lyase activity. Two N-terminal motifs, including a glutamine residue, are essential for conferring ACS activity to ACS-like proteins. Motif and activity analyses of ACS-like proteins from plants at different evolutionary stages suggest that the ACC-dependent pathway is uniquely developed in seed plants. A putative catalytic mechanism for the dual activities of ACSs is proposed on the basis of the crystal structure and biochemical data. These findings not only expand our current understanding of ACS functions but also provide novel insights into the evolutionary origin of ACS genes.
Controlled Subject
Molecular evolution
Disciplines
Molecular Biology | Molecular Genetics
File Format
File Size
3305 KB
Rights
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Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
Repository Citation
Xu, C.,
Hao, B.,
Sun, G.,
Mei, Y.,
Sun, L.,
Sun, Y.,
Wang, Y.,
Zhang, Y.,
Zhang, W.,
Zhang, M.,
Zhang, Y.,
Wang, D.,
Rao, Z.,
Li, X.,
Shen, J.,
Wang, N.
(2021).
Dual Activities of ACC Synthase: Novel Clues Regarding the Molecular Evolution of Acs Genes.
Science Advances, 7(46),
1-14.
Washington, D.C.: American Association for the Advancement of Science.
http://dx.doi.org/10.1126/sciadv.abg8752