Proteomics

Dataset Information

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Identification of AcpP-MukB binding sites using cross-linking mass spectrometry

ABSTRACT: Structural Maintenance of Chromosomes (SMC) complexes contribute ubiquitously to chromosome organization-segregation. SMC proteins have a conserved architecture, with a dimerization hinge and an ATPase head domain separated by a long antiparallel intramolecular coiled-coil. Dimeric SMC proteins interact with essential accessory proteins, kleisins that bridge the two subunits of an SMC dimer, and HAWK/KITE accessory proteins that interact with kleisins. The ATPase activity of the Escherichia coli SMC protein, MukB, is essential for in vivo function and is regulated by interactions with its dimeric kleisin, MukF, and KITE, MukE. Here we demonstrate that, in addition, MukB interacts with Acyl Carrier Protein (AcpP) that has essential functions in fatty acid synthesis. We characterize the AcpP interaction site at the joint of the MukB coiled-coil and show that the interaction is essential for MukB ATPase and for MukBEF function in vivo. Therefore, AcpP is an essential co-factor for MukBEF action in chromosome organization-segregation

INSTRUMENT(S): Q Exactive

ORGANISM(S): Escherichia Coli

SUBMITTER: Marjorie Fournier  

LAB HEAD: David Sherratt

PROVIDER: PXD026062 | Pride | 2021-11-25

REPOSITORIES: Pride

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Dataset's files

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Action DRS
MukBEF_AcpP_BS3.raw Raw
MukBEF_AcpP_BS3_XL.csv Csv
MukBEF_AcpP_BS3_proteins.csv Csv
MukBEF_BS3.raw Raw
MukBEF_BS3_XL.csv Csv
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Publications

Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation.

Prince Josh P JP   Bolla Jani R JR   Fisher Gemma L M GLM   Mäkelä Jarno J   Fournier Marjorie M   Robinson Carol V CV   Arciszewska Lidia K LK   Sherratt David J DJ  

Nature communications 20211118 1

Structural Maintenance of Chromosomes (SMC) complexes act ubiquitously to compact DNA linearly, thereby facilitating chromosome organization-segregation. SMC proteins have a conserved architecture, with a dimerization hinge and an ATPase head domain separated by a long antiparallel intramolecular coiled-coil. Dimeric SMC proteins interact with essential accessory proteins, kleisins that bridge the two subunits of an SMC dimer, and HAWK/KITE proteins that interact with kleisins. The ATPase activi  ...[more]

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