j 2023

The SDBC is active in quenching oxidative conditions and the cell in <i>Deinococcus radiodurans</i>

FARCI, Domenica, Andre T GRACA, Luca IESU, de Sanctis DANIELE, Dario PIANO et. al.

Basic information

Original name

The SDBC is active in quenching oxidative conditions and the cell in <i>Deinococcus radiodurans</i>

Authors

FARCI, Domenica (guarantor), Andre T GRACA, Luca IESU, de Sanctis DANIELE and Dario PIANO

Edition

International Journal of Biological Chemistry, AMSTERDAM, ANSInet, 2023, 1819-155X

Other information

Language

English

Type of outcome

Článek v odborném periodiku (nerecenzovaný)

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

RIV identification code

RIV/00216224:90242/23:00133745

DOI

UT WoS

001016293500001

Keywords in English

Deinococcus radiodurans; S-layer Deinoxanthin-binding complex; cryo-EM; superoxide dismutase (SOD);

Tags

Tags

International impact
Změněno: 11/4/2024 23:24, Mgr. Michal Petr

Abstract

V originále

Deinococcus radiodurans is known for its remarkable ability to withstand harsh stressful conditions. The outermost layer of its cell envelope is a proteinaceous coat, the S-layer, essential for resistance to and interactions with the environment. The S-layer Deinoxanthin-binding complex (SDBC), one of the main units of the characteristic multilayered cell envelope of this bacterium, protects against environmental stressors and allows exchanges with the environment. So far, specific regions of this complex, the collar and the stalk, remained unassigned. Here, these regions are resolved by cryo-EM and locally refined. The resulting 3D map shows that the collar region of this multiprotein complex is a trimer of the protein DR_0644, a Cu only superoxide dismutase (SOD) identified here to be efficient in quenching reactive oxygen species. The same data also showed that the stalk region consists of a coiled coil that extends into the cell envelope for 280 Å, reaching the inner membrane. Finally, the orientation and localization of the complex are defined by in situ cryo-electron crystallography. The structural organization of the SDBC couples fundamental UV antenna properties with the presence of a Cu-only SOD, showing here coexisting photoprotective and chemoprotective functions. These features suggests how the SDBC and similar protein complexes, might have played a primary role as evol utive templates for the origin of photoautotrophic processes by combining primary protective needs with more independent energetic strategies.

Links

90242, large research infrastructures
Name: CIISB III