A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA(+) Transcription Activator Protein PspF for Negative Regulation
Апстракт
To survive and colonise their various environments, including those used during infection, bacteria have developed a variety of adaptive systems. Amongst these is phage shock protein (Psp) response, which can be induced in Escherichia coli upon filamentous phage infection (specifically phage secretin pIV) and by other membrane-damaging agents. The E. coli Psp system comprises seven proteins, of which PspA is the central component. PspA is a bifunctional protein that is directly involved in (i) the negative regulation of the psp-specific transcriptional activator PspF and (ii) the maintenance of membrane integrity in a mechanism proposed to involve the formation of a 36-mer ring complex. Here we established that the PspA negative regulation of PspF ATPase activity is the result of a cooperative inhibition. We present biochemical evidence showing that an inhibitory PspA-PspF regulatory complex, which has significantly reduced PspF ATPase activity, is composed of around six PspF subunits ...and six PspA subunits, suggesting that PspA exists in at least two different oligomeric assemblies. We now establish that all four putative helical domains of PspA are critical for the formation of the 36-mer. In contrast, not all four helical domains are required for the formation of the inhibitory PspA-PspF complex. Since a range of initial PspF oligomeric states permit formation of the apparent PspA-PspF dodecameric assembly, we conclude that PspA and PspF demonstrate a strong propensity to self-assemble into a single defined heteromeric regulatory complex.
Кључне речи:
sigma(54) transcription / regulatory complex / PspF / PspA / phage shock protein (Psp)Извор:
Journal of Molecular Biology, 2009, 394, 4, 764-775Издавач:
- Academic Press Ltd- Elsevier Science Ltd, London
Финансирање / пројекти:
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council
- EMBO [ALTF 3872005]
- BBSRC [BB/G001278/1, BB/G00594X/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/G00594X/1, BB/G001278/1] Funding Source: researchfish
DOI: 10.1016/j.jmb.2009.09.055
ISSN: 0022-2836
PubMed: 19804784
WoS: 000272602900016
Scopus: 2-s2.0-70449521979
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Joly, Nicolas AU - Burrows, Patricia C. AU - Engl, Christoph AU - Jovanović, Goran AU - Buck, Martin PY - 2009 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/369 AB - To survive and colonise their various environments, including those used during infection, bacteria have developed a variety of adaptive systems. Amongst these is phage shock protein (Psp) response, which can be induced in Escherichia coli upon filamentous phage infection (specifically phage secretin pIV) and by other membrane-damaging agents. The E. coli Psp system comprises seven proteins, of which PspA is the central component. PspA is a bifunctional protein that is directly involved in (i) the negative regulation of the psp-specific transcriptional activator PspF and (ii) the maintenance of membrane integrity in a mechanism proposed to involve the formation of a 36-mer ring complex. Here we established that the PspA negative regulation of PspF ATPase activity is the result of a cooperative inhibition. We present biochemical evidence showing that an inhibitory PspA-PspF regulatory complex, which has significantly reduced PspF ATPase activity, is composed of around six PspF subunits and six PspA subunits, suggesting that PspA exists in at least two different oligomeric assemblies. We now establish that all four putative helical domains of PspA are critical for the formation of the 36-mer. In contrast, not all four helical domains are required for the formation of the inhibitory PspA-PspF complex. Since a range of initial PspF oligomeric states permit formation of the apparent PspA-PspF dodecameric assembly, we conclude that PspA and PspF demonstrate a strong propensity to self-assemble into a single defined heteromeric regulatory complex. PB - Academic Press Ltd- Elsevier Science Ltd, London T2 - Journal of Molecular Biology T1 - A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA(+) Transcription Activator Protein PspF for Negative Regulation EP - 775 IS - 4 SP - 764 VL - 394 DO - 10.1016/j.jmb.2009.09.055 ER -
@article{ author = "Joly, Nicolas and Burrows, Patricia C. and Engl, Christoph and Jovanović, Goran and Buck, Martin", year = "2009", abstract = "To survive and colonise their various environments, including those used during infection, bacteria have developed a variety of adaptive systems. Amongst these is phage shock protein (Psp) response, which can be induced in Escherichia coli upon filamentous phage infection (specifically phage secretin pIV) and by other membrane-damaging agents. The E. coli Psp system comprises seven proteins, of which PspA is the central component. PspA is a bifunctional protein that is directly involved in (i) the negative regulation of the psp-specific transcriptional activator PspF and (ii) the maintenance of membrane integrity in a mechanism proposed to involve the formation of a 36-mer ring complex. Here we established that the PspA negative regulation of PspF ATPase activity is the result of a cooperative inhibition. We present biochemical evidence showing that an inhibitory PspA-PspF regulatory complex, which has significantly reduced PspF ATPase activity, is composed of around six PspF subunits and six PspA subunits, suggesting that PspA exists in at least two different oligomeric assemblies. We now establish that all four putative helical domains of PspA are critical for the formation of the 36-mer. In contrast, not all four helical domains are required for the formation of the inhibitory PspA-PspF complex. Since a range of initial PspF oligomeric states permit formation of the apparent PspA-PspF dodecameric assembly, we conclude that PspA and PspF demonstrate a strong propensity to self-assemble into a single defined heteromeric regulatory complex.", publisher = "Academic Press Ltd- Elsevier Science Ltd, London", journal = "Journal of Molecular Biology", title = "A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA(+) Transcription Activator Protein PspF for Negative Regulation", pages = "775-764", number = "4", volume = "394", doi = "10.1016/j.jmb.2009.09.055" }
Joly, N., Burrows, P. C., Engl, C., Jovanović, G.,& Buck, M.. (2009). A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA(+) Transcription Activator Protein PspF for Negative Regulation. in Journal of Molecular Biology Academic Press Ltd- Elsevier Science Ltd, London., 394(4), 764-775. https://doi.org/10.1016/j.jmb.2009.09.055
Joly N, Burrows PC, Engl C, Jovanović G, Buck M. A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA(+) Transcription Activator Protein PspF for Negative Regulation. in Journal of Molecular Biology. 2009;394(4):764-775. doi:10.1016/j.jmb.2009.09.055 .
Joly, Nicolas, Burrows, Patricia C., Engl, Christoph, Jovanović, Goran, Buck, Martin, "A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA(+) Transcription Activator Protein PspF for Negative Regulation" in Journal of Molecular Biology, 394, no. 4 (2009):764-775, https://doi.org/10.1016/j.jmb.2009.09.055 . .