Extended structure of pleiotropic DNA repair‐promoting protein PprA from Deinococcus radiodurans. Issue 3 (27th November 2018)
- Record Type:
- Journal Article
- Title:
- Extended structure of pleiotropic DNA repair‐promoting protein PprA from Deinococcus radiodurans. Issue 3 (27th November 2018)
- Main Title:
- Extended structure of pleiotropic DNA repair‐promoting protein PprA from Deinococcus radiodurans
- Authors:
- Adachi, Motoyasu
Shimizu, Rumi
Shibazaki, Chie
Satoh, Katsuya
Fujiwara, Satoru
Arai, Shigeki
Narumi, Issay
Kuroki, Ryota - Abstract:
- ABSTRACT: Pleiotropic protein promoting DNA repair A (PprA) is a key protein facilitating the extreme radiation resistance of Deinococcus radiodurans . PprA is a unique protein to the genus Deinococcus and exists as an oligomer ranging from a tetramer to an ∼100‐mer depending on protein concentrations. Here, the X‐ray crystal structure of PprA was determined to clarify how PprA confers radiation resistance. The tertiary structure of dimeric PprA was elucidated by using mutants obtained with random and site‐directed mutagenesis methods (W183R and A139R); these mutants have disabled DNA binding and polymerization functions. Because the mutant A139R and W183R proteins have dimeric assemblies with 2 different interfaces (Interfaces 1 and 2), the linear and oligomerized PprA model was constructed as a left‐handed face‐to‐face periodic screw structure. In addition, the linear structure in solution was confirmed by small‐angle scattering experiments. The site‐directed mutational analysis identified essential basic amino acids for DNA binding. These analytical data support the hypothesis that a complex assembly of PprA molecules, which are extended and have a screw structure, surrounds and stretches the DNA strand, acting as a novel guide to colocalize the DNA strands for efficient DNA repairs.—Adachi, M., Shimizu, R., Shibazaki, C., Satoh, K., Fujiwara, S., Arai, S., Narumi, I., Kuroki, R. Extended structure of pleiotropic DNA repair‐promoting protein PprA from DeinococcusABSTRACT: Pleiotropic protein promoting DNA repair A (PprA) is a key protein facilitating the extreme radiation resistance of Deinococcus radiodurans . PprA is a unique protein to the genus Deinococcus and exists as an oligomer ranging from a tetramer to an ∼100‐mer depending on protein concentrations. Here, the X‐ray crystal structure of PprA was determined to clarify how PprA confers radiation resistance. The tertiary structure of dimeric PprA was elucidated by using mutants obtained with random and site‐directed mutagenesis methods (W183R and A139R); these mutants have disabled DNA binding and polymerization functions. Because the mutant A139R and W183R proteins have dimeric assemblies with 2 different interfaces (Interfaces 1 and 2), the linear and oligomerized PprA model was constructed as a left‐handed face‐to‐face periodic screw structure. In addition, the linear structure in solution was confirmed by small‐angle scattering experiments. The site‐directed mutational analysis identified essential basic amino acids for DNA binding. These analytical data support the hypothesis that a complex assembly of PprA molecules, which are extended and have a screw structure, surrounds and stretches the DNA strand, acting as a novel guide to colocalize the DNA strands for efficient DNA repairs.—Adachi, M., Shimizu, R., Shibazaki, C., Satoh, K., Fujiwara, S., Arai, S., Narumi, I., Kuroki, R. Extended structure of pleiotropic DNA repair‐promoting protein PprA from Deinococcus radiodurans . FASEB J. 33, 3647–3658 (2019). www.fasebj.org … (more)
- Is Part Of:
- FASEB journal. Volume 33:Issue 3(2019)
- Journal:
- FASEB journal
- Issue:
- Volume 33:Issue 3(2019)
- Issue Display:
- Volume 33, Issue 3 (2019)
- Year:
- 2019
- Volume:
- 33
- Issue:
- 3
- Issue Sort Value:
- 2019-0033-0003-0000
- Page Start:
- 3647
- Page End:
- 3658
- Publication Date:
- 2018-11-27
- Subjects:
- crystallography -- binding protein -- double-strand break -- radiation -- resistance
Biology -- Periodicals
Biology, Experimental -- Periodicals
570 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1096/fj.201801506R ↗
- Languages:
- English
- ISSNs:
- 0892-6638
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 13226.xml