Engagement of Arginine Finger to ATP Triggers Large Conformational Changes in NtrC1 AAA+ ATPase for Remodeling Bacterial RNA Polymerase

Baoyu Chen, Tatyana A. Sysoeva, Saikat Chowdhury, Liang Guo, Sacha De Carlo, Jeffrey A. Hanson, Haw Yang, B. Tracy Nixon

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

The NtrC-like AAA+ ATPases control virulence and other important bacterial activities through delivering mechanical work to σ54-RNA polymerase to activate transcription from σ54-dependent genes. We report the first crystal structure for such an ATPase, NtrC1 of Aquifex aeolicus, in which the catalytic arginine engages the γ-phosphate of ATP. Comparing the new structure with those previously known for apo and ADP-bound states supports a rigid-body displacement model that is consistent with large-scale conformational changes observed by low-resolution methods. First, the arginine finger induces rigid-body roll, extending surface loops above the plane of the ATPase ring to bind σ54. Second, ATP hydrolysis permits Pi release and retraction of the arginine with a reversed roll, remodeling σ54-RNAP. This model provides a fresh perspective on how ATPase subunits interact within the ring-ensemble to promote transcription, directing attention to structural changes on the arginine-finger side of an ATP-bound interface.

Original languageEnglish (US)
Pages (from-to)1420-1430
Number of pages11
JournalStructure
Volume18
Issue number11
DOIs
StatePublished - Nov 10 2010

Fingerprint

Bacterial RNA
DNA-Directed RNA Polymerases
Fingers
Adenosine Triphosphatases
Arginine
Adenosine Triphosphate
Adenosine Diphosphate
Virulence
Hydrolysis
Genes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Cite this

Chen, Baoyu ; Sysoeva, Tatyana A. ; Chowdhury, Saikat ; Guo, Liang ; De Carlo, Sacha ; Hanson, Jeffrey A. ; Yang, Haw ; Nixon, B. Tracy. / Engagement of Arginine Finger to ATP Triggers Large Conformational Changes in NtrC1 AAA+ ATPase for Remodeling Bacterial RNA Polymerase. In: Structure. 2010 ; Vol. 18, No. 11. pp. 1420-1430.
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Engagement of Arginine Finger to ATP Triggers Large Conformational Changes in NtrC1 AAA+ ATPase for Remodeling Bacterial RNA Polymerase. / Chen, Baoyu; Sysoeva, Tatyana A.; Chowdhury, Saikat; Guo, Liang; De Carlo, Sacha; Hanson, Jeffrey A.; Yang, Haw; Nixon, B. Tracy.

In: Structure, Vol. 18, No. 11, 10.11.2010, p. 1420-1430.

Research output: Contribution to journalArticle

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AU - Guo, Liang

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AU - Hanson, Jeffrey A.

AU - Yang, Haw

AU - Nixon, B. Tracy

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