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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Filaments and fingers: Novel structural aspects of the single septin from Chlamydomonas reinhardtii

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Author(s):
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Pinto, Andressa P. A. ; Pereira, Humberto M. ; Zeraik, Ana E. ; Ciol, Heloisa ; Ferreira, Frederico M. ; Brandao-Neto, Jose ; DeMarco, Ricardo ; Navarro, Marcos V. A. S. ; Risi, Cristina ; Galkin, Vitold E. ; Garratt, Richard C. ; Araujo, Ana P. U.
Total Authors: 12
Document type: Journal article
Source: Journal of Biological Chemistry; v. 292, n. 26, p. 10899-10911, JUN 30 2017.
Web of Science Citations: 2
Abstract

Septins are filament-forming GTP-binding proteins involved in many essential cellular events related to cytoskeletal dynamics and maintenance. Septins can self-assemble into heterocomplexes, which polymerize into highly organized, cell membrane-interacting filaments. The number of septin genes varies among organisms, and although their structure and function have been thoroughly studied in opisthokonts (including animals and fungi), no structural studies have been reported for other organisms. This makes the single septin from Chlamydomonas (CrSEPT) a particularly attractive model for investigating whether functional homopolymeric septin filaments also exist. CrSEPT was detected at the base of the flagella in Chlamydomonas, suggesting that CrSEPT is involved in the formation of a membrane-diffusion barrier. Using transmission electron microscopy, we observed that recombinant CrSEPT forms long filaments with dimensions comparable with those of the canonical structure described for opisthokonts. The GTP-binding domain of CrSEPT purified as a nucleotide-free monomer that hydrolyzes GTP and readily binds its analog guanosine 5'-3-O-(thio) triphosphate. We also found that upon nucleotide binding, CrSEPT formed dimers that were stabilized by an interface involving the ligand (G-interface). Across this interface, one monomer supplied a catalytic arginine to the opposing subunit, greatly accelerating the rate of GTP hydrolysis. This is the first report of an arginine finger observed in a septin and suggests that CrSEPT may act as its own GTP-activating protein. The finger is conserved in all algal septin sequences, suggesting a possible correlation between the ability to form homopolymeric filaments and the accelerated rate of hydrolysis that it provides. (AU)

FAPESP's process: 11/10152-7 - Structural and functional characterization of Chlamydomonas reinhardtii septin
Grantee:Ana Paula Ulian de Araujo
Support type: Regular Research Grants
FAPESP's process: 12/14223-9 - Structural and kinetical studies of the enzymes involved in the purine metabolism in Schistosoma mansoni
Grantee:Humberto D'Muniz Pereira
Support type: Regular Research Grants
FAPESP's process: 13/20715-4 - Studies of the correlation between septin dynamics and Ca2+ homeostasis in muscular cells from Schistosoma mansoni
Grantee:Ana Eliza Zeraik
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 12/21259-0 - Septin of Chlamydomonas reinhardtii: studies focusing its expression and function
Grantee:Heloisa Ciol
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 14/15546-1 - Septins: comparative studies and the correlation between structure and function
Grantee:Richard Charles Garratt
Support type: Research Projects - Thematic Grants