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(p)ppGpp controls stringent factors by exploiting antagonistic allosteric coupling between catalytic domains

ABSTRACT: Escherichia coli RelA is a ribosomal factor with strong (p)ppGpp synthesis activity that is dramatically activated in the presence of deacylated tRNA in the ribosomal A-site. RelA is a unique enzyme in that it is directly positively regulated by its product, alarmone nucleotide (p)ppGpp. Using HDX-MS, mulecular docking, biochemsitry, and microbiology approaches, we localise the (p)ppGpp binding site of E. coli RelA and uncover the molecular mechanism of RelA regulation by the alarmone.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Escherichia Coli

SUBMITTER: Simon Ekström

LAB HEAD: Vasili Hauryliuk

PROVIDER: PXD019953 | Pride | 2021-08-11

REPOSITORIES: Pride

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			Action	DRS
	HDExaminer_file.hdx	Other
	Individual_uptakeplots.pdf	Pdf
	Projectsummary.xlsx	Xlsx
	Rel_0_20181108_023235_0.raw	Raw
	Rel_3000_20181108_052732_3000.raw	Raw

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Transcriptome microarray of wildtype, relA, expI and rpoS Pectobacterium atrosepticum strains in PMB media

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