NDLI: A highly thermostable, homodimeric single-stranded DNA-binding protein from Deinococcus radiopugnans

Please wait, while we are loading the content...

Protein engineering of a cold-active β-galactosidase from Arthrobacter sp. SB to increase lactose hydrolysis reveals new sites affecting low temperature activity

Ferroplasma cupricumulans sp. nov., a novel moderately thermophilic, acidophilic archaeon isolated from an industrial-scale chalcocite bioleach heap

Salinicoccus salsiraiae sp. nov.: a new moderately halophilic gram-positive bacterium isolated from salted skate

Characterization of the cytoplasmic chaperonin containing TCP-1 from the Antarctic fish Notothenia coriiceps

Bacterial diversity in permanently cold and alkaline ikaite columns from Greenland

Polyphasic analysis of Thermus isolates from geothermal areas in Iceland

Life on the edge: hydrogen sulfide and the fish communities of a Mexican cave and surrounding waters

A novel thermostable sulfite oxidase from Thermus thermophilus: characterization of the enzyme, gene cloning and expression in Escherichia coli

An extracellular halophilic protease SptA from a halophilic archaeon Natrinema sp. J7: gene cloning, expression and characterization

A highly thermostable, homodimeric single-stranded DNA-binding protein from Deinococcus radiopugnans

Characterization of the Sulfolobus host–SSV2 virus interaction

Characterisation of the novel restriction endonuclease SuiI from Sulfolobus islandicus

Extremophiles : Volume 10, Issue 5, October 2006

Extremophiles : Volume 10, Issue 4, August 2006

Extremophiles : Volume 10, Issue 3, June 2006

Extremophiles : Volume 10, Issue 2, April 2006

Extremophiles : Volume 10, Issue 1, February 2006

Extremophiles : Volume 9

Extremophiles : Volume 8

Extremophiles : Volume 7

Extremophiles : Volume 6

Extremophiles : Volume 5

Extremophiles : Volume 4

Extremophiles : Volume 3

Extremophiles : Volume 2

Extremophiles : Volume 1

A highly thermostable, homodimeric single-stranded DNA-binding protein from Deinococcus radiopugnans

Content Provider	Springer Nature Link
Author	Filipkowski, Paweł Koziatek, Magdalena Kur, Józef
Copyright Year	2006
Abstract	We report the identification and characterization of the single-stranded DNA-binding protein (SSB) from the mesophile and highly radiation-resistant Deinococcus radiopugnans (DrpSSB). PCR-derived DNA fragment containing the complete structural gene for DrpSSB protein was cloned and expressed in Escherichia coli. The gene consisting of an open reading frame of 900 nucleotides encodes a protein of 300 amino acids with a calculated molecular weight of 32.45 kDa and pI 5.34. The amino acids sequence exhibits 43, 44, 79 and 18% identity with Thermus aquaticus, Thermus thermophilus, Deinococcus radiodurans and E. coli SSBs, respectively. The DrpSSB includes two OB folds per monomer and functions as a homodimer. In fluorescence titrations with poly(dT), DrpSSB bound 24–31 nt depending on the salt concentration, and fluorescence was quenched by about 80%. In a complementation assay in E. coli, DrpSSB took over the in vivo function of EcoSSB. The half-lives of DrpSSB were 120 min at 90°C, 60 min at 95°C and 30 min at 100°C. These results were surprising in the context of half-life of SSB from thermophilic T. aquaticus, which has only 30 s of half-life at 95°C. DrpSSB is the most thermostable SSB-like protein identified to date, offering an attractive alternative for TaqSSB and TthSSB in their applications for molecular biology methods and analytical purposes.
Starting Page	607
Ending Page	614
Page Count	8
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	10
Issue Number	6
e-ISSN	14334909
Language	English
Publisher	Springer-Verlag
Publisher Date	2006-08-02
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	DNA replication Expression Purification Thermophilic bacteria Thermostability Ecology Biotechnology Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The thermostability of DNA-binding protein HU from mesophilic, thermophilic, and extreme thermophilic bacteria

A highly thermostable trehalase from the thermophilic bacterium Rhodothermus marinus

Molecular cloning and expression of amylosucrase from highly radiation-resistant Deinococcus radiopugnans

Identification and characterization of a single-stranded DNA-binding protein from thermophilic bacteriophage GVE2

Thermostable lipases from the extreme thermophilic anaerobic bacteria Thermoanaerobacter thermohydrosulfuricus SOL1 and Caldanaerobacter subterraneus subsp. tengcongensis

Highly Thermostable Xylanase of the Thermophilic Fungus Talaromyces thermophilus: Purification and Characterization

A thermostable glucoamylase from a thermophilic Bacillus sp.: characterization and thermostability

Biochemical characterization of DNA-binding proteins from Pyrobaculum aerophilum and Aeropyrum pernix

The GINS complex from the thermophilic archaeon, Thermoplasma acidophilum may function as a homotetramer in DNA replication

A highly thermostable, homodimeric single-stranded DNA-binding protein from Deinococcus radiopugnans

Similar Documents

The thermostability of DNA-binding protein HU from mesophilic, thermophilic, and extreme thermophilic bacteria

A highly thermostable trehalase from the thermophilic bacterium Rhodothermus marinus

Molecular cloning and expression of amylosucrase from highly radiation-resistant Deinococcus radiopugnans

Identification and characterization of a single-stranded DNA-binding protein from thermophilic bacteriophage GVE2

Thermostable lipases from the extreme thermophilic anaerobic bacteria Thermoanaerobacter thermohydrosulfuricus SOL1 and Caldanaerobacter subterraneus subsp. tengcongensis

Highly Thermostable Xylanase of the Thermophilic Fungus Talaromyces thermophilus: Purification and Characterization

A thermostable glucoamylase from a thermophilic Bacillus sp.: characterization and thermostability

Biochemical characterization of DNA-binding proteins from Pyrobaculum aerophilum and Aeropyrum pernix

The GINS complex from the thermophilic archaeon, Thermoplasma acidophilum may function as a homotetramer in DNA replication

A highly thermostable, homodimeric single-stranded DNA-binding protein from Deinococcus radiopugnans