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Widespread PRC barrel proteins play critical roles in archaeal cell division.


ABSTRACT: Cell division is fundamental to all cellular life. Most of the archaea employ one of two alternative division machineries, one centered around the prokaryotic tubulin homolog FtsZ and the other around the endosomal sorting complex required for transport (ESCRT). However, neither of these mechanisms has been thoroughly characterized in archaea. Here, we show that three of the four PRC (Photosynthetic Reaction Center) barrel domain proteins of Haloferax volcanii (renamed Cell division proteins B1/2/3 (CdpB1/2/3)), play important roles in division. CdpB1 interacts directly with the FtsZ membrane anchor SepF and is essential for division, whereas deletion of cdpB2 and cdpB3 causes a major and a minor division defect, respectively. Orthologs of CdpB proteins are also involved in cell division in other haloarchaea. Phylogenetic analysis shows that PRC barrel proteins are widely distributed among archaea, including the highly conserved CdvA protein of the crenarchaeal ESCRT-based division system. Thus, diverse PRC barrel proteins appear to be central to cell division in most if not all archaea. Further study of these proteins is expected to elucidate the division mechanisms in archaea and their evolution.

SUBMITTER: Zhao S 

PROVIDER: S-EPMC10120694 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature

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Widespread PRC barrel proteins play critical roles in archaeal cell division.

Zhao Shan S   Makarova Kira S KS   Zheng Wenchao W   Liu Yafei Y   Zhan Le L   Wan Qianqian Q   Gong Han H   Krupovic Mart M   Lutkenhaus Joe J   Chen Xiangdong X   Koonin Eugene V EV   Du Shishen S  

bioRxiv : the preprint server for biology 20230328


Cell division is fundamental to all cellular life. Most of the archaea employ one of two alternative division machineries, one centered around the prokaryotic tubulin homolog FtsZ and the other around the endosomal sorting complex required for transport (ESCRT). However, neither of these mechanisms has been thoroughly characterized in archaea. Here, we show that three of the four PRC (Photosynthetic Reaction Center) barrel domain proteins of <i>Haloferax volcanii</i> (renamed Cell division prote  ...[more]

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