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The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red Alga Galdieria sulphuraria Co-assemble into Dynamic Filaments.

Publication ,  Journal Article
Chen, Y; Porter, K; Osawa, M; Augustus, AM; Milam, SL; Joshi, C; Osteryoung, KW; Erickson, HP
Published in: J Biol Chem
March 31, 2017

FtsZ is a homolog of eukaryotic tubulin and is present in almost all bacteria and many archaea, where it is the major cytoskeletal protein in the Z ring, required for cell division. Unlike some other cell organelles of prokaryotic origin, chloroplasts have retained FtsZ as an essential component of the division machinery. However, chloroplast FtsZs have been challenging to study because they are difficult to express and purify. To this end, we have used a FATT tag expression system to produce as soluble proteins the two chloroplast FtsZs from Galdieria sulphuraria, a thermophilic red alga. GsFtsZA and GsFtsZB assembled individually in the presence of GTP, forming large bundles of protofilaments. GsFtsZA also assembled in the presence of GDP, the first member of the FtsZ/tubulin superfamily to do so. Mixtures of GsFtsZA and GsFtsZB assembled protofilament bundles and hydrolyzed GTP at a rate approximately equal to the sum of their individual rates, suggesting a random co-assembly. GsFtsZA assembly by itself in limiting GTP gave polymers that remained stable for a prolonged time. However, when GsFtsZB was added, the co-polymers disassembled with enhanced kinetics, suggesting that the GsFtsZB regulates and enhances disassembly dynamics. GsFtsZA-mts (where mts is a membrane-targeting amphipathic helix) formed Z ring-like helices when expressed in Escherichia coli Co-expression of GsFtsZB (without an mts) gave co-assembly of both into similar helices. In summary, we provide biochemical evidence that GsFtsZA assembles as the primary scaffold of the chloroplast Z ring and that GsFtsZB co-assembly enhances polymer disassembly and dynamics.

Duke Scholars

Published In

J Biol Chem

DOI

EISSN

1083-351X

Publication Date

March 31, 2017

Volume

292

Issue

13

Start / End Page

5207 / 5215

Location

United States

Related Subject Headings

  • Tubulin
  • Structural Homology, Protein
  • Rhodophyta
  • Kinetics
  • Guanosine Triphosphate
  • Cytoskeleton
  • Cytoskeletal Proteins
  • Chloroplasts
  • Biochemistry & Molecular Biology
  • Bacterial Proteins
 

Citation

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Chen, Y., Porter, K., Osawa, M., Augustus, A. M., Milam, S. L., Joshi, C., … Erickson, H. P. (2017). The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red Alga Galdieria sulphuraria Co-assemble into Dynamic Filaments. J Biol Chem, 292(13), 5207–5215. https://doi.org/10.1074/jbc.M116.767715
Chen, Yaodong, Katie Porter, Masaki Osawa, Anne Marie Augustus, Sara L. Milam, Chandra Joshi, Katherine W. Osteryoung, and Harold P. Erickson. “The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red Alga Galdieria sulphuraria Co-assemble into Dynamic Filaments.J Biol Chem 292, no. 13 (March 31, 2017): 5207–15. https://doi.org/10.1074/jbc.M116.767715.
Chen Y, Porter K, Osawa M, Augustus AM, Milam SL, Joshi C, et al. The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red Alga Galdieria sulphuraria Co-assemble into Dynamic Filaments. J Biol Chem. 2017 Mar 31;292(13):5207–15.
Chen, Yaodong, et al. “The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red Alga Galdieria sulphuraria Co-assemble into Dynamic Filaments.J Biol Chem, vol. 292, no. 13, Mar. 2017, pp. 5207–15. Pubmed, doi:10.1074/jbc.M116.767715.
Chen Y, Porter K, Osawa M, Augustus AM, Milam SL, Joshi C, Osteryoung KW, Erickson HP. The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red Alga Galdieria sulphuraria Co-assemble into Dynamic Filaments. J Biol Chem. 2017 Mar 31;292(13):5207–5215.

Published In

J Biol Chem

DOI

EISSN

1083-351X

Publication Date

March 31, 2017

Volume

292

Issue

13

Start / End Page

5207 / 5215

Location

United States

Related Subject Headings

  • Tubulin
  • Structural Homology, Protein
  • Rhodophyta
  • Kinetics
  • Guanosine Triphosphate
  • Cytoskeleton
  • Cytoskeletal Proteins
  • Chloroplasts
  • Biochemistry & Molecular Biology
  • Bacterial Proteins