Cyanobacterial carboxysomes contain an unique rubisco-activase-like protein.

Autor: Lechno-Yossef S; MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA.; Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA., Rohnke BA; MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA.; Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA., Belza ACO; MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA., Melnicki MR; MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA., Montgomery BL; MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA.; Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA.; Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI, 48824, USA., Kerfeld CA; MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA.; Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA.; Environmental Genomics and Systems Biology and Molecular Biophysics and Integrated Bioimaging Divisions, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Jazyk: angličtina
Zdroj: The New phytologist [New Phytol] 2020 Jan; Vol. 225 (2), pp. 793-806. Date of Electronic Publication: 2019 Oct 25.
DOI: 10.1111/nph.16195
Abstrakt: In plants, rubisco activase (Rca) regulates rubisco by removing inhibitory molecules such as ribulose-1,5-bisphosphate (RuBP). In cyanobacteria, a homologous protein (activase-like cyanobacterial protein, ALC), contains a distinctive C-terminal fusion resembling the small-subunit of rubisco. Although cyanobacterial rubisco is believed to be less sensitive to RuBP inhibition, the ALC is widely distributed among diverse cyanobacteria. Using microscopy, biochemistry and molecular biology, the cellular localization of the ALC, its effect on carboxysome/cell ultrastructure in Fremyella diplosiphon, and its function in vitro were studied. Bioinformatic analysis uncovered evolutionary relationships between the ALC and rubisco. ALC localizes to carboxysomes and exhibits ATPase activity. Furthermore, the ALC induces rubisco aggregation in a manner similar to that of another carboxysomal protein, M35, and this activity is affected by ATP. An alc deletion mutant showed modified cell morphology when grown under enriched CO 2 and impaired regulation of carboxysome biogenesis, without affecting growth rate. Carbamylation of Fremyella recombinant rubisco was inhibited by RuBP, but this inhibition was not relieved by the ALC. The ALC does not appear to function like a canonical Rca; instead, it exerts an effect on the response to CO 2 availability at the level of a metabolic module, the carboxysome, through rubisco network formation, and carboxysome organization.
(© 2019 The Authors. New Phytologist © 2019 New Phytologist Trust.)
Databáze: MEDLINE
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