Recombinant Escherichia coli Psp operon transcriptional activator (pspF)

1. identified the minimal PspF-interacting domain of PspA, solved its structure, determined its affinity to PspF and the dissociation kinetics, identified residues that are potentially important for PspF regulation and analyzed effects of their mutation on PspF in vivo and in vitro PMID: 26235546
2. By comparing the properties of the log and stationary phases, we find that the dynamics of PspF are influenced by the growth phase and may be controlled by the changes in the cytoplasmic fluidity. PMID: 25849912
3. By structural modelling, authors propose that PspA binds to PspF via its first two helical domains. PMID: 23659791
4. Identification of two previously unknown PspF loop 1 (L1)-binding patches within region 1 of sigma54. PMID: 22772990
5. The transcription activator PspF is a molecular model whose conserved amino acid residues have roles in ATP hydrolysis and intersubunit communication. PMID: 22789710
6. The phage shock protein (Psp) stress response system is an important part of the stress response machinery in Escherichia coli K12. PMID: 21059793
7. determined by cryogenic electron microscopy a 20 angstrom resolution structure of PspF(1-275) which is bound to an ATP transition state analog in complex with its basal factor, sigma54; identified two loops involved in binding sigma54 PMID: 15790859
8. A bacterial two-hybrid system allowed us to provide clear evidence for an interaction in E. coli between PspA and PspF in vivo, which strongly suggests that PspA-directed inhibition of PspF occurs via an inhibitory complex. PMID: 15838051
9. Results propose a putative atomic switch that is responsible for coupling structural changes in the nucleotide-binding site to the repositioning of the sigma(54)-interacting loops of PspF. PMID: 16430918
10. 6S RNA at elevated pH limits the extent of the psp response under conditions of nutrient deprivation, facilitating appropriate allocation of diminishing resources. PMID: 16707685
11. A stochastic nucleotide binding and a coordinated hydrolysis mechanism in PspF1-275 hexamers is presented. PMID: 16973614
12. PspF hydrolysis is relayed via Thr(148) to loop 2 creating motions that provide mechanical force to the GAFTGA loop 1 that contacts sigma(54)-RNA polymerase. PMID: 17242399
13. analysis of how PspF couples ATPase activity in AAA+ proteins for transcription activation PMID: 18326037
14. The pre-SIi loop in PspF is a major structural feature mediating nucleotide state-dependent differential engagement with Esigma54. PMID: 19486295
15. Here the authors established that the PspA negative regulation of PspF ATPase activity is the result of a cooperative inhibition. PMID: 19804784

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KEGG: ecj:JW1296

STRING: 316385.ECDH10B_1420