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Identification of the bacteriophage nucleus protein interaction network

ABSTRACT: Here, we use proximity labeling and localization mapping to systematically identify proteins associated with the major nuclear shell protein chimallin (ChmA) and other distinctive structures assembled by these phages. We identify six uncharacterized nuclear shell-associated proteins, one of which directly interacts with self-assembled ChmA. The structure and protein-protein interaction network of this protein, which we term ChmB, suggests that it forms pores in the ChmA lattice that serve as docking sites for pro-capsid genome packaging, and may also participate in mRNA and/or protein transport.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Pseudomonas Phage Phipa3

SUBMITTER: Eray Enustun

LAB HEAD: Kevin Corbett

PROVIDER: PXD041684 | Pride | 2024-01-26

REPOSITORIES: Pride

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			Action	DRS
	Biotin_1_gP53_ON_biotin_infected_QPA3.mgf	Mgf
	Biotin_GPA3.mgf	Mgf
	EE_biotin_010.mgf	Mgf
	EE_biotin_03.mgf	Mgf
	GFP-mini-1.mgf	Mgf

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Publications

Identification of the bacteriophage nucleus protein interaction network.

Enustun Eray E Deep Amar A Gu Yajie Y Nguyen Katrina T KT Chaikeeratisak Vorrapon V Armbruster Emily E Ghassemian Majid M Villa Elizabeth E Pogliano Joe J Corbett Kevin D KD

Nature structural & molecular biology 20230904 11

In the arms race between bacteria and bacteriophages (phages), some large-genome jumbo phages have evolved a protein shell that encloses their replicating genome to protect it against host immune factors. By segregating the genome from the host cytoplasm, however, the 'phage nucleus' introduces the need to specifically translocate messenger RNA and proteins through the nuclear shell and to dock capsids on the shell for genome packaging. Here, we use proximity labeling and localization mapping to ...[more]

PMID: 37667030

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Proteomic analysis of the shell organic matrix of Spondylus Gaederopus

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