Journal Article

PUBDB-2018-05473

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Recombinant production of A1S_0222 from Acinetobacter baumannii ATCC 17978 and confirmation of its DNA-(adenine N6)-methyltransferase activity

Blaschke, U.Extern* ; Suwono, B. ; Zafari, S. ; Ebersberger, I. ; Skiebe, E. ; Jeffries, C. M.Extern* ; Svergun, D. I.EMBL* ; Wilharm, G. (Corresponding author)

2018
Elsevier Amsterdam [u.a.]

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Please use a persistent id in citations: doi:10.1016/j.pep.2018.06.009  doi:10.3204/PUBDB-2018-05473

Abstract: 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.

Note: © Elsevier Inc.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)
2. EMBL (EMBL)

Research Program(s):

1. 6G3 - PETRA III (POF3-622) (POF3-622)

Experiment(s):

1. PETRA Beamline P12 (PETRA III)

Appears in the scientific report 2018

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Database coverage:
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