Zobrazeno 1 - 10
of 200
pro vyhledávání: '"Claudio O. Gualerzi"'
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 24, p 13238 (2021)
Substitution of the conserved Histidine 448 present in one of the three consensus elements characterizing the guanosine nucleotide binding domain (IF2 G2) of Escherichia coli translation initiation factor IF2 resulted in impaired ribosome-dependent G
Externí odkaz:
https://doaj.org/article/e533c42ee55140ab87c119ada977a3fd
Autor:
Jerneja Tomsic, Arianna Smorlesi, Enrico Caserta, Anna Maria Giuliodori, Cynthia L. Pon, Claudio O. Gualerzi
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 3, p 735 (2020)
The conserved Histidine 301 in switch II of Geobacillus stearothermophilus IF2 G2 domain was substituted with Ser, Gln, Arg, Leu and Tyr to generate mutants displaying different phenotypes. Overexpression of IF2H301S, IF2H301L and IF2H301Y in cells e
Externí odkaz:
https://doaj.org/article/702bd5f38d604ee1aa3c9446b5c6dfca
Autor:
David Bulkley, Letizia Brandi, Yury S. Polikanov, Attilio Fabbretti, Michael O’Connor, Claudio O. Gualerzi, Thomas A. Steitz
Publikováno v:
Cell Reports, Vol 6, Iss 2, Pp 357-365 (2014)
The translocation of mRNA and tRNA through the ribosome is catalyzed by elongation factor G (EF-G), a universally conserved guanosine triphosphate hydrolase (GTPase). The mechanism by which the closely related decapeptide antibiotics dityromycin and
Externí odkaz:
https://doaj.org/article/0eef0a3e96dd4781ba82132d2fc7a839
Publikováno v:
Antibiotics, Vol 5, Iss 2, p 17 (2016)
GE81112 is a tetrapeptide antibiotic that binds to the 30S ribosomal subunit and specifically inhibits P-site decoding of the mRNA initiation codon by the fMet-tRNA anticodon. GE81112 displays excellent microbiological activity against some Gram-posi
Externí odkaz:
https://doaj.org/article/dccf27c922844d34abfda33636c8daf0
Publikováno v:
Encyclopedia of Biological Chemistry III ISBN: 9780128220405
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d60df9ac9aae919b32e31774b62a0604
https://doi.org/10.1016/b978-0-12-819460-7.00278-4
https://doi.org/10.1016/b978-0-12-819460-7.00278-4
Autor:
Claudio O. Gualerzi, Anna Maria Giuliodori, Enrico Caserta, Arianna Smorlesi, Cynthia L. Pon, Jerneja Tomšic
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 3, p 735 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 3
International Journal of Molecular Sciences
Volume 21
Issue 3
The conserved Histidine 301 in switch II of Geobacillus stearothermophilus IF2 G2 domain was substituted with Ser, Gln, Arg, Leu and Tyr to generate mutants displaying different phenotypes. Overexpression of IF2H301S, IF2H301L and IF2H301Y in cells e
Autor:
Jerneja, Tomsic, Arianna, Smorlesi, Enrico, Caserta, Anna Maria, Giuliodori, Cynthia L, Pon, Claudio O, Gualerzi
Publikováno v:
International Journal of Molecular Sciences
The conserved Histidine 301 in switch II of Geobacillus stearothermophilus IF2 G2 domain was substituted with Ser, Gln, Arg, Leu and Tyr to generate mutants displaying different phenotypes. Overexpression of IF2H301S, IF2H301L and IF2H301Y in cells e
Autor:
Frank Schmidt, Claudio O. Gualerzi, Anna Brandi, Lolita Piersimoni, Roberto Spurio, Jean-Hervé Alix, Naser Aliye Feto
Publikováno v:
Nucleic Acids Research
Cold-stress in Escherichia coli induces de novo synthesis of translation initiation factors IF1, IF2 and IF3 while ribosome synthesis and assembly slow down. Consequently, the IFs/ribosome stoichiometric ratio increases about 3-fold during the first
Autor:
Anna Brandi, Mara Giangrossi, Anna Maria Giuliodori, Claudio O. Gualerzi, Cynthia L. Pon, Silvia Paoloni, Roberto Spurio
Publikováno v:
Nucleic Acids Research
After a 37 to 10°C temperature downshift the level of translation initiation factor IF2, like that of IF1 and IF3, increases at least 3-fold with respect to the ribosomes. To clarify the mechanisms and conditions leading to cold-stress induction of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86a03d59d8e9f70c1fa83eb589c8677b
http://hdl.handle.net/11581/426034
http://hdl.handle.net/11581/426034
Publikováno v:
International Journal of Molecular Sciences
Volume 20
Issue 3
International Journal of Molecular Sciences, Vol 20, Iss 3, p 457 (2019)
Volume 20
Issue 3
International Journal of Molecular Sciences, Vol 20, Iss 3, p 457 (2019)
In Escherichia coli, the mRNA transcribed from the main cold-shock gene cspA is a thermosensor, which at low temperature adopts a conformation particularly suitable for translation in the cold. Unlike cspA, its paralogue cspD is expressed only at 37