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Insights into ParB spreading from the complex structure of Spo0J and parS
- Source :
- Proceedings of the National Academy of Sciences. 112:6613-6618
- Publication Year :
- 2015
- Publisher :
- Proceedings of the National Academy of Sciences, 2015.
-
Abstract
- Spo0J (stage 0 sporulation protein J, a member of the ParB superfamily) is an essential component of the ParABS (partition system of ParA, ParB, and parS)-related bacterial chromosome segregation system. ParB (partition protein B) and its regulatory protein, ParA, act cooperatively through parS (partition S) DNA to facilitate chromosome segregation. ParB binds to chromosomal DNA at specific parS sites as well as the neighboring nonspecific DNA sites. Various ParB molecules can associate together and spread along the chromosomal DNA. ParB oligomer and parS DNA interact together to form a high-order nucleoprotein that is required for the loading of the structural maintenance of chromosomes proteins onto the chromosome for chromosomal DNA condensation. In this report, we characterized the binding of parS and Spo0J from Helicobacter pylori (HpSpo0J) and solved the crystal structure of the C-terminal domain truncated protein (Ct-HpSpo0J)-parS complex. Ct-HpSpo0J folds into an elongated structure that includes a flexible N-terminal domain for protein-protein interaction and a conserved DNA-binding domain for parS binding. Two Ct-HpSpo0J molecules bind with one parS. Ct-HpSpo0J interacts vertically and horizontally with its neighbors through the N-terminal domain to form an oligomer. These adjacent and transverse interactions are accomplished via a highly conserved arginine patch: RRLR. These interactions might be needed for molecular assembly of a high-order nucleoprotein complex and for ParB spreading. A structural model for ParB spreading and chromosomal DNA condensation that lead to chromosome segregation is proposed.
- Subjects :
- DNA, Bacterial
Models, Molecular
Molecular Sequence Data
Plasma protein binding
Biology
Crystallography, X-Ray
Chromosome segregation
chemistry.chemical_compound
Bacterial Proteins
X-Ray Diffraction
Chromosome Segregation
Scattering, Small Angle
Protein Interaction Domains and Motifs
Amino Acid Sequence
Protein Structure, Quaternary
Peptide sequence
Spores, Bacterial
Genetics
Regulation of gene expression
Multidisciplinary
Base Sequence
Helicobacter pylori
Sequence Homology, Amino Acid
Circular bacterial chromosome
Chromosome
Biological Sciences
Cell biology
Nucleoprotein
chemistry
DNA
Protein Binding
Subjects
Details
- ISSN :
- 10916490 and 00278424
- Volume :
- 112
- Database :
- OpenAIRE
- Journal :
- Proceedings of the National Academy of Sciences
- Accession number :
- edsair.doi.dedup.....af742e4c2ef45d3f421ed415309f994a