Evolution of Ycf54-independent chlorophyll biosynthesis in cyanobacteria
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F21%3A43903672" target="_blank" >RIV/60076658:12310/21:43903672 - isvavai.cz</a>
Alternative codes found
RIV/60077344:_____/21:00552505 RIV/61388971:_____/21:00544888
Result on the web
<a href="https://www.pnas.org/content/118/10/e2024633118" target="_blank" >https://www.pnas.org/content/118/10/e2024633118</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1073/pnas.2024633118" target="_blank" >10.1073/pnas.2024633118</a>
Alternative languages
Result language
angličtina
Original language name
Evolution of Ycf54-independent chlorophyll biosynthesis in cyanobacteria
Original language description
Chlorophylls (Chls) are essential cofactors for photosynthesis. One of the least understood steps of Chl biosynthesis is formation of the fifth (E) ring, where the red substrate, magnesium protoporphyrin IX monomethyl ester, is converted to the green product, 3,8-divinyl protochlorophyllide a. In oxygenic phototrophs, this reaction is catalyzed by an oxygen-dependent cyclase, consisting of a catalytic subunit (AcsF/CycI) and an auxiliary protein, Ycf54. Deletion of Ycf54 impairs cyclase activity and results in severe Chl deficiency, but its exact role is not clear. Here, we used a.ycf54 mutant of the model cyanobacterium Synechocystis sp. PCC 6803 to generate suppressor mutations that restore normal levels of Chl. Sequencing.ycf54 revertants identified a single D219G amino acid substitution in CycI and frameshifts in slr1916, which encodes a putative esterase. Introduction of these mutations to the original.ycf54 mutant validated the suppressor effect, especially in combination. However, comprehensive analysis of the.ycf54 suppressor strains revealed that the D219G-substituted CycI is only partially active and its accumulation is misregulated, suggesting that Ycf54 controls both the level and activity of CycI. We also show that Slr1916 has Chl dephytylase activity in vitro and its inactivation up-regulates the entire Chl biosynthetic pathway, resulting in improved cyclase activity. Finally, large-scale bioinformatic analysis indicates that our laboratory evolution of Ycf54-independent CycI mimics natural evolution of AcsF in low-light-adapted ecotypes of the oceanic cyanobacteria Prochlorococcus, which lack Ycf54, providing insight into the evolutionary history of the cyclase enzyme.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/GX19-29225X" target="_blank" >GX19-29225X: Intertwined biogenesis of photosystems I and II: born together to work together</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Proceedings of The National Academy of Sciences of The United States of America
ISSN
0027-8424
e-ISSN
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Volume of the periodical
118
Issue of the periodical within the volume
10
Country of publishing house
US - UNITED STATES
Number of pages
12
Pages from-to
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UT code for WoS article
000627429100102
EID of the result in the Scopus database
2-s2.0-85102328508