Back to Search
Start Over
Dynamic Interaction of the Escherichia coli Cell Division ZipA and FtsZ Proteins Evidenced in Nanodiscs
- Source :
- Journal of Biological Chemistry; Vol 287, Digital.CSIC. Repositorio Institucional del CSIC, instname, Journal of Biological Chemistry
- Publication Year :
- 2012
- Publisher :
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2012.
-
Abstract
- The full-length ZipA protein from Escherichia coli, one of the essential components of the division proto-ring that provides membrane tethering to the septation FtsZ protein, has been incorporated in single copy into nanodiscs formed by a membrane scaffold protein encircling an E. coli phospholipid mixture. This is an acellular system that reproduces the assembly of part of the cell division components. ZipA contained in nanodiscs (Nd-ZipA) retains the ability to interact with FtsZ oligomers and with FtsZ polymers. Interactions with FtsZ occur at similar strengths as those involved in the binding of the soluble form of ZipA, lacking the transmembrane region, suggesting that the transmembrane region of ZipA has little influence on the formation of the ZipA·plex. Peptides containing partial sequences of the C terminus of FtsZ compete with FtsZ polymers for binding to Nd-ZipA. The affinity of Nd-ZipA for the FtsZ polymer formed with GTP or GMPCPP (a slowly hydrolyzable analog of GTP) is moderate (micromolar range) and of similar magnitude as for FtsZ-GDP oligomers. Polymerization does not stabilize the binding of FtsZ to ZipA. This supports the role of ZipA as a passive anchoring device for the proto-ring with little implication, if any, in the regulation of its assembly. Furthermore, it indicates that the tethering of FtsZ to the membrane shows sufficient plasticity to allow for its release from noncentral regions of the cytoplasmic membrane and its subsequent relocation to midcell when demanded by the assembly of a division ring.
- Subjects :
- Scaffold protein
Cell division
Cell Cycle Proteins
macromolecular substances
physiological processes
Biochemistry
Protein–protein interaction
Cell membrane
03 medical and health sciences
Bacterial Proteins
Escherichia coli
medicine
Protein Structure, Quaternary
FtsZ
Cytoskeleton
Molecular Biology
030304 developmental biology
0303 health sciences
biology
Escherichia coli Proteins
C-terminus
Cell Membrane
030302 biochemistry & molecular biology
Cell Biology
Protein Structure, Tertiary
Cell biology
Cytoskeletal Proteins
medicine.anatomical_structure
Cytoplasm
Multiprotein Complexes
biology.protein
bacteria
Protein Multimerization
biological phenomena, cell phenomena, and immunity
Carrier Proteins
Cell Division
Molecular Biophysics
Subjects
Details
- Language :
- English
- ISSN :
- 1083351X
- Volume :
- 287
- Issue :
- 36
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....5d8ac8c98b28ceb7e8acbe76e395f69e
- Full Text :
- https://doi.org/10.1074/jbc.M112.388959