Comparison of the DING protein from the archaeon Sulfolobus solfataricus with human phosphate-binding protein and Pseudomonas fluorescence DING counterparts

Autor: Teresa Ricciardi, Elena Porzio, Giuseppe Manco, Maria Rosaria Faraone-Mennella, Anna De Maio, Carmela Mistretta

Publikováno v: Extremophiles. 22:177-188

DING proteins represent a new group of 40 kDa-related members, ubiquitous in living organisms. The family also include the DING protein from Sulfolobus solfataricus, functionally related to poly(ADP-ribose) polymerases. Here, the archaeal protein has

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5d7ae68a2139934353ee04ac042b71e
https://doi.org/10.1007/s00792-017-0985-4

Crystal structure of a thermophilic O6-alkylguanine-DNA alkyltransferase-derived self-labeling protein-tag in covalent complex with a fluorescent probe

Autor: Castrese Morrone, Franca Rossi, Davide M. Ferraris, Anna Valenti, Giuseppe Perugino, Alberto Massarotti, Riccardo Miggiano

Publikováno v: Biochemical and biophysical research communications
500 (2018): 698–703. doi:10.1016/j.bbrc.2018.04.139
info:cnr-pdr/source/autori:Rossi, Franca; Morrone, Castrese; Massarotti, Alberto; Ferraris, Davide Maria; Valenti, Anna; Perugino, Giuseppe; Miggiano, Riccardo/titolo:Crystal structure of a thermophilic O-6-alkylguanine-DNA alkyltransferase-derived self-labeling protein-tag in covalent complex with a fluorescent probe/doi:10.1016%2Fj.bbrc.2018.04.139/rivista:Biochemical and biophysical research communications (Print)/anno:2018/pagina_da:698/pagina_a:703/intervallo_pagine:698–703/volume:500

The self-labeling protein tags are robust and versatile tools for studying different molecular aspects of cell biology. In order to be suitable for a wide spectrum of experimental conditions, it is mandatory that these systems are stable after the fl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98b743beafd7bccac7cb7748219c6000
http://hdl.handle.net/11588/893317

Inhibition of translesion DNA polymerase by archaeal reverse gyrase

Autor: Anna Valenti, Giuseppe Perugino, Maria Ciaramella, Takehiko Nohmi, Mosè Rossi

Publikováno v: Nucleic acids research 37 (2009): 4287–4295. doi:10.1093/nar/gkp386
info:cnr-pdr/source/autori:Valenti A.; Perugino G.; Nohmi T.; Rossi M.; Ciaramella M./titolo:Inhibition of translesion DNA polymerase by archaeal reverse gyrase/doi:10.1093%2Fnar%2Fgkp386/rivista:Nucleic acids research/anno:2009/pagina_da:4287/pagina_a:4295/intervallo_pagine:4287–4295/volume:37
Nucleic Acids Research

Reverse gyrase is a unique DNA topoisomerase endowed with ATP-dependent positive supercoiling activity. It is typical of microorganisms living at high temperature and might play a role in maintenance of genome stability and repair. We have identified

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45c2e4a8dfb4c1e6147626e473666c4b
https://doi.org/10.1093/nar/gkp386

Evidence that the xylanase activity from Sulfolobus solfataricus Oα is encoded by the endoglucanase precursor gene (sso1354) and characterization of the associated cellulase activity

Autor: Immacolata Fiume, Marco Moracci, Mosè Rossi, Alessandra Esposito, Alessandra Morana, Alfonso Giovane, Luisa Maurelli

Publikováno v: Extremophiles (Tokyo, Print) 12 (2008): 689–700. doi:10.1007/s00792-008-0175-5
info:cnr-pdr/source/autori:Maurelli L.; Giovane A.; Esposito A.; Moracci M.; Fiume I.; Rossi M.; Morana A./titolo:Evidence that the xylanase activity from Sulfolobus solfataricus O alpha is encoded by the endoglucanase precursor gene (sso1354) and characterisation of the associated cellulase activity/doi:10.1007%2Fs00792-008-0175-5/rivista:Extremophiles (Tokyo, Print)/anno:2008/pagina_da:689/pagina_a:700/intervallo_pagine:689–700/volume:12

Sulfolobus solfataricus strain Oalpha was previously isolated for its ability to grow on minimal medium supplemented with xylan as a carbon source. The strain exhibited thermostable xylanase activity but several attempts to identify the gene encoding

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79c7caf796f17652086e75fb24036aeb
https://doi.org/10.1007/s00792-008-0175-5

Multiple disulfide bridges modulate conformational stability and flexibility in hyperthermophilic archaeal purine nucleoside phosphorylase

Autor: Giovanna Cacciapuoti, Elisa Martino, Georges Feller, Maria Libera Bagarolo, Marina Porcelli

5′-Deoxy-5′-methylthioadenosine phosphorylase from Sulfolobus solfataricus is a hexameric hyperthermophilic protein containing in each subunit two pairs of disulfide bridges, a CXC motif, and one free cysteine. The contribution of each disulfide

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ec3bdae52d17c7f14950dc685f81164
http://hdl.handle.net/11591/332345