Sulfolobus solfataricus N-terminus and other regions of the partial amino acid sequence of a thermoprotein exhibiting poly(ADP-ribose) polymerase activity suggest that it belongs to the DINGGG class of proteins that are often described as membrane bound. Our previous biochemical studies demonstrated that the thermoprotein is also strictly associated with DNA, and is only partially solubilized from cell homogenate. The present research is focused on the analysis of the sulfolobal DING thermozyme localization within the archaeal cell.

The DINGGG thermoprotein is membrane bound in the Crenarchaeon Sulfolobus solfataricus / Porzio, Elena; Bianchi, ANNA RITA; Baccigalupi, Loredana; Isticato, Rachele; FARAONE MENNELLA, MARIA ROSARIA. - In: CHEMICAL AND BIOLOGICAL TECHNOLOGIES IN AGRICULTURE. - ISSN 2196-5641. - 3:3(2016), pp. 1-8. [10.1186/s40538-016-0055-7]

The DINGGG thermoprotein is membrane bound in the Crenarchaeon Sulfolobus solfataricus

PORZIO, ELENA;BIANCHI, ANNA RITA;BACCIGALUPI, LOREDANA;ISTICATO, RACHELE;FARAONE MENNELLA, MARIA ROSARIA
2016

Abstract

Sulfolobus solfataricus N-terminus and other regions of the partial amino acid sequence of a thermoprotein exhibiting poly(ADP-ribose) polymerase activity suggest that it belongs to the DINGGG class of proteins that are often described as membrane bound. Our previous biochemical studies demonstrated that the thermoprotein is also strictly associated with DNA, and is only partially solubilized from cell homogenate. The present research is focused on the analysis of the sulfolobal DING thermozyme localization within the archaeal cell.
2016
The DINGGG thermoprotein is membrane bound in the Crenarchaeon Sulfolobus solfataricus / Porzio, Elena; Bianchi, ANNA RITA; Baccigalupi, Loredana; Isticato, Rachele; FARAONE MENNELLA, MARIA ROSARIA. - In: CHEMICAL AND BIOLOGICAL TECHNOLOGIES IN AGRICULTURE. - ISSN 2196-5641. - 3:3(2016), pp. 1-8. [10.1186/s40538-016-0055-7]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/645109
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