Zobrazeno 1 - 10
of 114
pro vyhledávání: '"toxin-antitoxin module"'
Publikováno v:
Frontiers in Microbiology, Vol 12 (2021)
Externí odkaz:
https://doaj.org/article/158a6e84065a4ee0ab01402d46b102b8
Autor:
Tilman Schirmer, Tjaart A. P. de Beer, Stefanie Tamegger, Alexander Harms, Nikolaus Dietz, David M. Dranow, Thomas E. Edwards, Peter J. Myler, Isabelle Phan, Christoph Dehio
Publikováno v:
Microorganisms, Vol 9, Iss 8, p 1645 (2021)
Proteins containing a FIC domain catalyze AMPylation and other post-translational modifications (PTMs). In bacteria, they are typically part of FicTA toxin-antitoxin modules that control conserved biochemical processes such as topoisomerase activity,
Externí odkaz:
https://doaj.org/article/0c0a04bb822f444e9e906df589ade52f
Publikováno v:
AIMS Microbiology, Vol 3, Iss 2, Pp 171-185 (2017)
Bacterial persistence is a state of metabolic dormancy among a small fraction (
Externí odkaz:
https://doaj.org/article/a1faf31eb5304030badf5be5bb5a772b
Autor:
Hanna Sprenger, Sabine Kienesberger, Brigitte Pertschy, Lisa Pöltl, Bettina Konrad, Priya Bhutada, Dina Vorkapic, Denise Atzmüller, Florian Feist, Christoph Högenauer, Gregor Gorkiewicz, Ellen L. Zechner
Publikováno v:
Frontiers in Microbiology, Vol 8 (2017)
Enzymes containing the FIC (filamentation induced by cyclic AMP) domain catalyze post-translational modifications of target proteins. In bacteria the activity of some Fic proteins resembles classical toxin–antitoxin (TA) systems. An excess of toxin
Externí odkaz:
https://doaj.org/article/cf847491e3394c1e97223633c383bd09
Autor:
Safia Zedek, Remy Loris, Pieter De Bruyn, Thomas Jové, Daniel Charlier, Frédéric Goormaghtigh, Alexandra Vandervelde, Nathan Fraikin, Dukas Jurėnas, Laurence Van Melderen
Publikováno v:
mBio
mBio, Vol 12, Iss 6 (2021)
mBio, Vol 12, Iss 6 (2021)
Type II toxin-antitoxin (TA) systems are classically composed of two genes that encode a toxic protein and a cognate antitoxin protein. Both genes are organized in an operon whose expression is autoregulated at the level of transcription by the antit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bc4e6d76937c19c6fa824eb2b61b37f
https://pubmed.ncbi.nlm.nih.gov/34844426
https://pubmed.ncbi.nlm.nih.gov/34844426
Autor:
Frank Sobott, Pieter De Bruyn, Els Pardon, Jan Steyaert, Milan Malfait, Maruša Prolič-Kalinšek, Yann G.-J. Sterckx, Alexandra Vandervelde, Remy Loris, San Hadži
Publikováno v:
Acta Chrystallographica Section F
Acta Crystallogr F Struct Biol Commun
Acta Crystallogr F Struct Biol Commun
paaR2–paaA2–parE2 is a three-component toxin–antitoxin module found in prophage CP-993P of Escherichia coli O157:H7. Transcription regulation of this module occurs via the 123-amino-acid regulator PaaR2, which forms a large oligomeric structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a3dbb9d07c99618a357700fb193806d
https://eprints.whiterose.ac.uk/180323/6/S2053230X21009006.pdf
https://eprints.whiterose.ac.uk/180323/6/S2053230X21009006.pdf
Autor:
Dukas Jurėnas, Remy Loris, Pieter De Bruyn, Laurence Van Melderen, Maruša Prolič-Kalinšek, Alexander N. Volkov
Publikováno v:
Biomolecular N M R Assignments
The cryptic prophage CP-933P in Escherichia coli O157:H7 contains a parDE-like toxin–antitoxin module, the operator region of which is recognized by two flanking transcription regulators: PaaR2 (ParE associated Regulator), which forms part of the p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30825048ca3252b54e5426b84ad67bb0
https://doi.org/10.1007/s12104-019-09915-9
https://doi.org/10.1007/s12104-019-09915-9
Autor:
Schirmer, Tilman, de Beer, Tjaart A. P., Tamegger, Stefanie, Harms, Alexander, Dietz, Nikolaus, Dranow, David M., Edwards, Thomas E., Myler, Peter J., Phan, Isabelle, Dehio, Christoph
Publikováno v:
Microorganisms, 9 (8)
Microorganisms
Volume 9
Issue 8
Microorganisms, Vol 9, Iss 1645, p 1645 (2021)
Microorganisms
Volume 9
Issue 8
Microorganisms, Vol 9, Iss 1645, p 1645 (2021)
Proteins containing a FIC domain catalyze AMPylation and other post-translational modifications (PTMs). In bacteria, they are typically part of FicTA toxin-antitoxin modules that control conserved biochemical processes such as topoisomerase activity,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62311fe2891c363f9ec3ed62faa11506
https://hdl.handle.net/20.500.11850/603815
https://hdl.handle.net/20.500.11850/603815
Autor:
Garcia Rodriguez, Gabriela, Girardin, Yana, Volkov, Oleksandr, Singh, Ranjan Kumar, Muruganandam, Gopinath, Van Dyck, Jeroen, Sobott, Frank, Versees, Wim, Charlier, Daniel, Loris, Remy
ParD2 is the antitoxin component of the parDE2 toxin-antitoxin module from Vibrio cholerae and consists of an ordered DNA binding domain followed by an intrinsically disordered ParE-neutralizing domain. In absence of the C-terminal IDP domain, VcParD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______3848::c4e8fc708123c90309b8a749ce755ffa
https://doi.org/10.1107/s2059798321004873
https://doi.org/10.1107/s2059798321004873
Publikováno v:
'Nucleic Acids Research ', vol: 49, pages: 7164-7178 (2021)
Nucleic Acids Research
Nucleic Acids Research
The rnlAB toxin-antitoxin operon from Escherichia coli functions as an anti-phage defense system. RnlA was recently identified as a member of the HEPN (Higher Eukaryotes and Prokaryotes Nucleotide-binding domain) superfamily of ribonucleases. The act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d735896f710d22bf2017fc21449e277c
https://lirias.kuleuven.be/handle/123456789/676609
https://lirias.kuleuven.be/handle/123456789/676609