A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Dps-like proteins: structural and functional insights into a versatile protein family
Tekijät: Haikarainen T, Papageorgiou AC
Kustantaja: BIRKHAUSER VERLAG AG
Julkaisuvuosi: 2010
Journal: Cellular and Molecular Life Sciences
Tietokannassa oleva lehden nimi: CELLULAR AND MOLECULAR LIFE SCIENCES
Lehden akronyymi: CELL MOL LIFE SCI
Vuosikerta: 67
Numero: 3
Aloitussivu: 341
Lopetussivu: 351
Sivujen määrä: 11
ISSN: 1420-682X
DOI: https://doi.org/10.1007/s00018-009-0168-2
Tiivistelmä
Dps-like proteins are key factors involved in the protection of prokaryotic cells from oxidative damage. They act by either oxidizing iron to prevent the formation of oxidative radicals or by forming Dps-DNA complexes to physically protect DNA. All Dps-like proteins are characterized by a common three-dimensional architecture and are found as spherical dodecamers with a hollow central cavity. Despite their structural similarities, recent biochemical and structural data have suggested different functions among members of the family that range from protection inside the cells in response to various stress signals to adhesion and virulence during bacterial infections. Moreover, the Dps-like proteins have lately attracted considerable interest in the field of nanotechnology owing to their ability to act as protein cages for iron and various other metals. A better understanding of their function and mechanism could therefore lead to novel applications in biotechnology and nanotechnology.
Dps-like proteins are key factors involved in the protection of prokaryotic cells from oxidative damage. They act by either oxidizing iron to prevent the formation of oxidative radicals or by forming Dps-DNA complexes to physically protect DNA. All Dps-like proteins are characterized by a common three-dimensional architecture and are found as spherical dodecamers with a hollow central cavity. Despite their structural similarities, recent biochemical and structural data have suggested different functions among members of the family that range from protection inside the cells in response to various stress signals to adhesion and virulence during bacterial infections. Moreover, the Dps-like proteins have lately attracted considerable interest in the field of nanotechnology owing to their ability to act as protein cages for iron and various other metals. A better understanding of their function and mechanism could therefore lead to novel applications in biotechnology and nanotechnology.
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