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The structural basis for the self-inhibition of DNA binding by apo-σ70 - CLMS data

ABSTRACT: Performing crosslinking mass spectrometry and intergrative structural modelling to elucidate, for the first time, structure models of apo-σ70. Conclusively, we provide structural information to show that most of the DNA-binding capabilities of apo-σ70 are conformationally-inhibited and can be activated mostly in the context of transcription. CL-MS performed in E. coli detects crosslinks unique to the compact fold of apo-σ70 occurring at stationary growth phase.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Escherichia Coli

SUBMITTER: Khalil Joron

LAB HEAD: Eitan Lerner

PROVIDER: PXD037183 | Pride | 2022-10-13

REPOSITORIES: Pride

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			Action	DRS
	In_vitro_BS3_Sigma70_1st_repeat_P4.msf	Msf
	In_vitro_BS3_Sigma70_1st_repeat_P4.raw	Raw
	In_vitro_BS3_Sigma70_2nd_repeat_P4.msf	Msf
	In_vitro_BS3_Sigma70_2nd_repeat_P4.raw	Raw
	In_vitro_BS3_Sigma70_3rd_repeat_P4.msf	Msf

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