Zobrazeno 1 - 10 of 12 pro vyhledávání: '"Martino Morici"'
1
Akademický článek
RAPP-containing arrest peptides induce translational stalling by short circuiting the ribosomal peptidyltransferase activity
Autor: Martino Morici, Sara Gabrielli, Keigo Fujiwara, Helge Paternoga, Bertrand Beckert, Lars V. Bock, Shinobu Chiba, Daniel N. Wilson
Publikováno v: Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract Arrest peptides containing RAPP (ArgAlaProPro) motifs have been discovered in both Gram-positive and Gram-negative bacteria, where they are thought to regulate expression of important protein localization machinery components. Here we determ
Externí odkaz: https://doaj.org/article/7bb148fa3087456198fc966a68df11f9
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2
Akademický článek
The SecM arrest peptide traps a pre-peptide bond formation state of the ribosome
Autor: Felix Gersteuer, Martino Morici, Sara Gabrielli, Keigo Fujiwara, Haaris A. Safdari, Helge Paternoga, Lars V. Bock, Shinobu Chiba, Daniel N. Wilson
Publikováno v: Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract Nascent polypeptide chains can induce translational stalling to regulate gene expression. This is exemplified by the E. coli secretion monitor (SecM) arrest peptide that induces translational stalling to regulate expression of the downstream
Externí odkaz: https://doaj.org/article/73596d597f1f42cfaa8ac810322d5c48
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5
Structural basis for translation inhibition by the glycosylated drosocin peptide
Autor: Timm O. Koller, Martino Morici, Max Berger, Haaris A. Safdari, Deepti S. Lele, Bertrand Beckert, Kanwal J. Kaur, Daniel N. Wilson
Publikováno v: Nature Chemical Biology.
The proline-rich antimicrobial peptide (PrAMP) drosocin is produced by Drosophila species to combat bacterial infection. Unlike many PrAMPs, drosocin is O-glycosylated at threonine 11, a post-translation modification that enhances its antimicrobial a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f36fd0bf7230bab434e4f99837205f81
https://doi.org/10.1038/s41589-023-01293-7
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6
Structural basis for translation inhibition by the glycosylated antimicrobial peptide Drosocin fromDrosophila melanogaster
Autor: Timm O. Koller, Martino Morici, Max Berger, Haaris A. Safdari, Deepti S. Lele, Bertrand Beckert, Kanwal J. Kaur, Daniel N. Wilson
The proline-rich antimicrobial peptide (PrAMP) drosocin is produced byDrosophilaspecies to combat bacterial infection. Unlike many PrAMPs, drosocin is O-glycosylated at threonine 11, a post-translation modification that enhances its antimicrobial act
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::46add49385df3535b986d14c1a62825c
https://doi.org/10.1101/2022.12.08.519698
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7
The cyclic octapeptide antibiotic argyrin B inhibits translation by trapping EF-G on the ribosome during translocation
Autor: Maximiliane Wieland, Mikael Holm, Emily J. Rundlet, Martino Morici, Timm O. Koller, Tinashe P. Maviza, Domen Pogorevc, Ilya A. Osterman, Rolf Müller, Scott C. Blanchard, Daniel N. Wilson
Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 119(19)
Argyrins are a family of naturally produced octapeptides that display promising antimicrobial activity against Pseudomonas aeruginosa. Argyrin B (ArgB) has been shown to interact with an elongated form of the translation elongation factor G (EF-G), l
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21ba16944e0196313ba255a0c8813cf0
https://pubmed.ncbi.nlm.nih.gov/35500116
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