The helicase DinG responds to stress due to DNA double strand breaks.

Autor: Stephan A Frye, Getachew Tesfaye Beyene, Amine Namouchi, Marta Gómez-Muñoz, Håvard Homberset, Shewit Kalayou, Tahira Riaz, Tone Tønjum, Seetha V Balasingham

Publikováno v: PLoS ONE, Vol 12, Iss 11, p e0187900 (2017)

Neisseria meningitidis (Nm) is a Gram-negative nasopharyngeal commensal that can cause septicaemia and meningitis. The neisserial DNA damage-inducible protein DinG is a helicase related to the mammalian helicases XPD and FANCJ. These helicases belong

Externí odkaz: https://doaj.org/article/c1d52ee2e74647d8b87466474089556e

The Inner Membrane Protein PilG Interacts with DNA and the Secretin PilQ in Transformation.

Autor: Stephan A Frye, Emma Lång, Getachew Tesfaye Beyene, Seetha V Balasingham, Håvard Homberset, Alexander D Rowe, Ole Herman Ambur, Tone Tønjum

Publikováno v: PLoS ONE, Vol 10, Iss 8, p e0134954 (2015)

Expression of type IV pili (Tfp), filamentous appendages emanating from the bacterial surface, is indispensable for efficient neisserial transformation. Tfp pass through the secretin pore consisting of the membrane protein PilQ. PilG is a polytopic m

Externí odkaz: https://doaj.org/article/92f43c8ecd1c4098829952528c28f5f2

DprA from Neisseria meningitidis: properties and role in natural competence for transformation

Autor: Ole Herman Ambur, Håvard Homberset, Eirik Hovland, Tone Tønjum, Marta Gómez-Muñoz, Jeremy P. Derrick, Getachew Tesfaye Beyene, Stephan A. Frye, Seetha V. Balasingham

Publikováno v: Microbiology
Hovland, E, Beyene, G T, Frye, S A, Homberset, H, Balasingham, S V, Gómez-Muñoz, M, Derrick, J P, Tønjum, T & Ambur, O H 2017, ' DprA from Neisseria meningitidis : Properties and role in natural competence for transformation ', Microbiology, vol. 163, no. 7, pp. 1016-1029 . https://doi.org/10.1099/mic.0.000489

DNA processing chain A (DprA) is a DNA-binding protein that is ubiquitous in bacteria and expressed in some archaea. DprA is active in many bacterial species that are competent for transformation of DNA, but its role in Neisseriameningitidis (Nm) is

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7de033522650227b831d44048ab3de45
https://pubmed.ncbi.nlm.nih.gov/28696187

Effects of conserved residues and naturally occurring mutations on Mycobacterium tuberculosis RecG helicase activity

Autor: Håvard Homberset, Ephrem Debebe Zegeye, Per Eugen Kristiansen, Seetha V. Balasingham, Tone Tønjum, Jon K. Laerdahl

Publikováno v: Microbiology. 160:217-227

RecG is a helicase that is conserved in nearly all bacterial species. The prototypicalEscherichia coliRecG promotes regression of stalled replication forks, participates in DNA recombination and DNA repair, and prevents aberrant replication.Mycobacte

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7a6747c82ebb4aa8e7f2b7581aaa848
https://doi.org/10.1099/mic.0.072140-0

Mycobacterium tuberculosis RecG binds and unwinds model DNA substrates with a preference for Holliday junctions

Autor: Håvard Homberset, Seetha V. Balasingham, Ephrem Debebe Zegeye, Tone Tønjum, Jon K. Laerdahl

Publikováno v: Microbiology

The RecG enzyme, a superfamily 2 helicase, is present in nearly all bacteria. Here we report for the first time that the recG gene is also present in the genomes of most vascular plants as well as in green algae, but is not found in other eukaryotes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f08de265854d69f28fb718149181f4ae
https://doi.org/10.1099/mic.0.058693-0