The DNA Alkylguanine DNA Alkyltransferase-2 (AGT-2) Of Caenorhabditis Elegans Is Involved In Meiosis And Early Development Under Physiological Conditions

Autor: Maria Ciaramella, Adele Adamo, Giuseppe Perugino, Noemi Russo, Mario Serpe, Chiara Forenza, Anna Valenti

Publikováno v: Scientific Reports
Scientific reports (Nature Publishing Group) (2019). doi:10.1038/s41598-019-43394-1
info:cnr-pdr/source/autori:Mario Serpe, Chiara Forenza, Adele Adamo, Noemi Russo, Giuseppe Perugino, Maria Ciaramella & Anna Valenti/titolo:The DNA Alkylguanine DNA Alkyltransferase-2 (AGT-2) Of Caenorhabditis Elegans Is Involved In Meiosis And Early Development Under Physiological Conditions/doi:10.1038%2Fs41598-019-43394-1/rivista:Scientific reports (Nature Publishing Group)/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume
Scientific Reports, Vol 9, Iss 1, Pp 1-15 (2019)

DNA alkylguanine DNA alkyltransferases (AGTs) are evolutionary conserved proteins that repair alkylation damage in DNA, counteracting the effects of agents inducing such lesions. Over the last years AGTs have raised considerable interest for both the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae491e9ad745427fdaf55dae1451074c
https://doi.org/10.1038/s41598-019-43394-1

Chromatin Structure and Dynamics in Hot Environments: Architectural Proteins and DNA Topoisomerases of Thermophilic Archaea

Autor: Antonella Vettone, Mario Serpe, Giuseppe Perugino, Valeria Visone, Mosè Rossi, Maria Ciaramella, Anna Valenti

Publikováno v: International Journal of Molecular Sciences, Vol 15, Iss 9, Pp 17162-17187 (2014)
International Journal of Molecular Sciences
International journal of molecular sciences
15 (2014): 17162–17187.
info:cnr-pdr/source/autori:V. Visone, A. Vettone, M. Serpe, A. Valenti, G. Perugino, M. Rossi and M. Ciaramella/titolo:Chromatin structure and dynamics in hot environment: architectural proteins and DNA topoisomerases of thermophilic archaea/doi:/rivista:International journal of molecular sciences (Print)/anno:2014/pagina_da:17162/pagina_a:17187/intervallo_pagine:17162–17187/volume:15

In all organisms of the three living domains (Bacteria, Archaea, Eucarya) chromosome-associated proteins play a key role in genome functional organization. They not only compact and shape the genome structure, but also regulate its dynamics, which is

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae69ad512aa9ce1dc632b67cc357968f
http://www.mdpi.com/1422-0067/15/9/17162

Interdomain interactions rearrangements control the reaction steps of a thermostable DNA alkyltransferase

Autor: Maria Ciaramella, Riccardo Miggiano, Menico Rizzi, Mario Serpe, Anna Valenti, Mosè Rossi, Giuseppe Perugino, Alberto Massarotti, Franca Rossi, Castrese Morrone, Giovanni del Monaco

Publikováno v: Biochimica et biophysica acta
1861 (2017): 86–96. doi:10.1016/j.bbagen.2016.10.020
info:cnr-pdr/source/autori:Morrone C, Miggiano R, Serpe M, Massarotti A, Valenti A, Del Monaco G, Rossi M, Rossi F, Rizzi M, Perugino G, Ciaramella M./titolo:Interdomain interactions rearrangements control the reaction steps of a thermostable DNA alkyltransferase./doi:10.1016%2Fj.bbagen.2016.10.020/rivista:Biochimica et biophysica acta (Print)/anno:2017/pagina_da:86/pagina_a:96/intervallo_pagine:86–96/volume:1861

Background Alkylated DNA-protein alkyltransferases (AGTs) are conserved proteins that repair alkylation damage in DNA by using a single-step mechanism leading to irreversible alkylation of the catalytic cysteine in the active site. Trans-alkylation i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bf4e79e50246874aea57098f5699772
https://pubmed.ncbi.nlm.nih.gov/27777086

A novel thermostable protein-tag: optimization of the Sulfolobus solfataricus DNA- alkyl-transferase by protein engineering

Autor: Antonella Vettone, Mario Serpe, Aurelio Hidalgo, José Berenguer, Giovanni del Monaco, Anna Valenti, Mosé Rossi, Maria Ciaramella, Giuseppe Perugino

Publikováno v: Extremophiles (Tokyo, Print) 20 (2016): 1–13. doi:10.1007/s00792-015-0791-9
info:cnr-pdr/source/autori:Vettone A.; Serpe M.; Hidalgo A.; Berenguer J.; Del Monaco G.; Valenti A.; Rossi M.; Ciaramella M.; Perugino G./titolo:A novel thermostable protein-tag: optimization of the Sulfolobus solfataricus DNA-alkyl-transferase by protein engineering/doi:10.1007%2Fs00792-015-0791-9/rivista:Extremophiles (Tokyo, Print)/anno:2016/pagina_da:1/pagina_a:13/intervallo_pagine:1–13/volume:20
Europe PubMed Central

In the last decade, a powerful biotechnological tool for the in vivo and in vitro specific labeling of proteins (SNAP-tag(TM) technology) was proposed as a valid alternative to classical protein-tags (green fluorescent proteins, GFPs). This was made

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4aef2f91b70788d3eeae3fb8a1a7d069
https://pubmed.ncbi.nlm.nih.gov/26666951