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TitleRecombinant production of A1S_0222 from Acinetobacter baumannii ATCC 17978 and confirmation of its DNA-(adenine N6)-methyltransferase activity.
Journal, issue, pagesProtein Expr Purif, Vol. 151, Page 78-85, Year 2018
Publish dateJun 22, 2018
AuthorsUlrike Blaschke / Beneditta Suwono / Sachli Zafari / Ingo Ebersberger / Evelyn Skiebe / Cy M Jeffries / Dmitri I Svergun / Gottfried Wilharm /
PubMed AbstractAcinetobacter baumannii appears as an often multidrug-resistant nosocomial pathogen in hospitals worldwide. Its remarkable persistence in the hospital environment is probably due to intrinsic and ...Acinetobacter baumannii appears as an often multidrug-resistant nosocomial pathogen in hospitals worldwide. Its remarkable persistence in the hospital environment is probably due to intrinsic and acquired resistance to disinfectants and antibiotics, tolerance to desiccation stress, capability to form biofilms, and is possibly facilitated by surface-associated motility. Our attempts to elucidate surface-associated motility in A. baumannii revealed a mutant inactivated in a putative DNA-(adenine N6)-methyltransferase, designated A1S_0222 in strain ATCC 17978. We recombinantly produced A1S_0222 as a glutathione S-transferase (GST) fusion protein and purified it to near homogeneity through a combination of GST affinity chromatography, cation exchange chromatography and PD-10 desalting column. Furthermore we demonstrate A1S_0222-dependent adenine methylation at a GAATTC site. We propose the name AamA (Acinetobacteradenine methyltransferase A) in addition to the formal names M.AbaBGORF222P/M.Aba17978ORF8565P. Small angle X-ray scattering (SAXS) revealed that the protein is monomeric and has an extended and likely two-domain shape in solution.
External linksProtein Expr Purif / PubMed:29908915
MethodsSAS (X-ray synchrotron)
Structure data

SASDD32:
DNA-(adenine N6)-methyltransferase from Acinetobacter baumannii ATCC 17978
Method: SAXS/SANS

Source
  • Acinetobacter baumannii atcc 17978 (bacteria)

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