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Pregled bibliografske jedinice broj: 462503

Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases


Husain, Nilofer; Tkaczuk, Karolina L; Tulsidas, Shenoy Rajesh; Kaminska, Katarzyna H.; Čubrilo, Sonja; Maravić Vlahoviček, Gordana; Bujnicki, Janusz M.; Sivaraman, Jayaraman
Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases // Nucleic acids research, 38 (2010), 12; 4120-4132 doi:10.1093/nar/gkq122 (međunarodna recenzija, članak, znanstveni)


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Naslov
Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases

Autori
Husain, Nilofer ; Tkaczuk, Karolina L ; Tulsidas, Shenoy Rajesh ; Kaminska, Katarzyna H. ; Čubrilo, Sonja ; Maravić Vlahoviček, Gordana ; Bujnicki, Janusz M. ; Sivaraman, Jayaraman

Izvornik
Nucleic acids research (0305-1048) 38 (2010), 12; 4120-4132

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
antibiotic resistance; methyltransferase; Sgm; aminoglycosides; gentamicin; sisomicin

Sažetak
Sgm (Sisomicin-gentamicin methyltransferase) from antibiotic-producing bacterium Micromonospora zionensis is an enzyme that confers resistance to aminoglycosides like gentamicin and sisomicin by specifically methylating G1405 in bacterial 16S rRNA. Sgm belongs to the aminoglycoside resistance methyltransferase (Arm) family of enzymes that have been recently found to spread by horizontal gene transfer among disease-causing bacteria. Structural characterization of Arm enzymes is the key to understand their mechanism of action and to develop inhibitors that would block their activity. Here we report the structure of Sgm in complex with cofactors S-adenosylmethionine (AdoMet) and S-adenosylhomocysteine (AdoHcy) at 2.0 and 2.1 Å resolution, respectively, and results of mutagenesis and rRNA footprinting, and protein-substrate docking. We propose the mechanism of methylation of G1405 by Sgm and compare it with other m7G methyltransferases, revealing a surprising diversity of active sites and binding modes for the same basic reaction of RNA modification. This analysis can serve as a stepping stone towards developing drugs that would specifically block the activity of Arm methyltransferases and thereby re-sensitize pathogenic bacteria to aminoglycoside antibiotics.

Izvorni jezik
Engleski

Znanstvena područja
Biologija



POVEZANOST RADA


Projekti:
006-0982913-1219 - Molekularne osnove djelovanja antibiotika i mehanizmi bakterijske rezistencije (Maravić Vlahoviček, Gordana, MZOS ) ( CroRIS)

Ustanove:
Farmaceutsko-biokemijski fakultet, Zagreb

Poveznice na cjeloviti tekst rada:

doi nar.oxfordjournals.org nar.oxfordjournals.org

Citiraj ovu publikaciju:

Husain, Nilofer; Tkaczuk, Karolina L; Tulsidas, Shenoy Rajesh; Kaminska, Katarzyna H.; Čubrilo, Sonja; Maravić Vlahoviček, Gordana; Bujnicki, Janusz M.; Sivaraman, Jayaraman
Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases // Nucleic acids research, 38 (2010), 12; 4120-4132 doi:10.1093/nar/gkq122 (međunarodna recenzija, članak, znanstveni)
Husain, N., Tkaczuk, K., Tulsidas, S., Kaminska, K., Čubrilo, S., Maravić Vlahoviček, G., Bujnicki, J. & Sivaraman, J. (2010) Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases. Nucleic acids research, 38 (12), 4120-4132 doi:10.1093/nar/gkq122.
@article{article, author = {Husain, Nilofer and Tkaczuk, Karolina L and Tulsidas, Shenoy Rajesh and Kaminska, Katarzyna H. and \v{C}ubrilo, Sonja and Maravi\'{c} Vlahovi\v{c}ek, Gordana and Bujnicki, Janusz M. and Sivaraman, Jayaraman}, year = {2010}, pages = {4120-4132}, DOI = {10.1093/nar/gkq122}, keywords = {antibiotic resistance, methyltransferase, Sgm, aminoglycosides, gentamicin, sisomicin}, journal = {Nucleic acids research}, doi = {10.1093/nar/gkq122}, volume = {38}, number = {12}, issn = {0305-1048}, title = {Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases}, keyword = {antibiotic resistance, methyltransferase, Sgm, aminoglycosides, gentamicin, sisomicin} }
@article{article, author = {Husain, Nilofer and Tkaczuk, Karolina L and Tulsidas, Shenoy Rajesh and Kaminska, Katarzyna H. and \v{C}ubrilo, Sonja and Maravi\'{c} Vlahovi\v{c}ek, Gordana and Bujnicki, Janusz M. and Sivaraman, Jayaraman}, year = {2010}, pages = {4120-4132}, DOI = {10.1093/nar/gkq122}, keywords = {antibiotic resistance, methyltransferase, Sgm, aminoglycosides, gentamicin, sisomicin}, journal = {Nucleic acids research}, doi = {10.1093/nar/gkq122}, volume = {38}, number = {12}, issn = {0305-1048}, title = {Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases}, keyword = {antibiotic resistance, methyltransferase, Sgm, aminoglycosides, gentamicin, sisomicin} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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