New insights into structural and functional relationships between LonA proteases and ClpB chaperones

Rotanova, Tatyana V.; Andrianova, Anna G.; Kudzhaev, Arsen M.; Li, Mi; Botos, Istvan; Wlodawer, Alexander; Gustchina, Alla

doi:10.1002/2211-5463.12691

Title: New insights into structural and functional relationships between LonA proteases and ClpB chaperones

Journal Article · Tue Jun 25 00:00:00 EDT 2019 · FEBS Open Bio

DOI:https://doi.org/10.1002/2211-5463.12691· OSTI ID:1562698

Rotanova, Tatyana V. ^[1]; Andrianova, Anna G. ^[1]; Kudzhaev, Arsen M. ^[1]; Li, Mi ^[2]; Botos, Istvan ^[3]; Wlodawer, Alexander ^[4]; Gustchina, Alla ^[4]

Russian Academy of Sciences, Moscow (Russia)
National Cancer Institute, Frederick, MD (United States); Frederick National Lab. for Cancer Research, Frederick, MD (United States)
National Inst. of Diabetes and Digestive and Kidney Diseases, Bethesda, MD (United States)
National Cancer Institute, Frederick, MD (United States

LonA proteases and ClpB chaperones are key components of the protein quality control system in bacterial cells. LonA proteases form a unique family of ATPases associated with diverse cellular activities (AAA⁺) proteins due to the presence of an unusual N-terminal region comprised of two domains: a β-structured N domain and an α-helical domain, including the coiled-coil fragment, which is referred to as HI(CC). The arrangement of helices in the HI(CC) domain is reminiscent of the structure of the H1 domain of the first AAA⁺ module of ClpB chaperones. It has been hypothesized that LonA proteases with a single AAA⁺ module may also contain a part of another AAA⁺ module, the full version of which is present in ClpB. Here, we established and tested the structural basis of this hypothesis using the known crystal structures of various fragments of LonA proteases and ClpB chaperones, as well as the newly determined structure of the Escherichia coli LonA fragment (235–584). The similarities and differences in the corresponding domains of LonA proteases and ClpB chaperones were examined in structural terms. The results of our analysis, complemented by the finding of a singular match in the location of the most conserved axial pore-1 loop between the LonA NB domain and the NB2 domain of ClpB, support our hypothesis that there is a structural and functional relationship between two coiled–coil fragments and implies a similar mechanism of engagement of the pore-1 loops in the AAA⁺ modules of LonAs and ClpBs.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE; National Cancer Institute (NCI); National Institutes of Health (NIH); Russian Foundation for Basic Research

Grant/Contract Number:: HHSN261200800001E; 19-04-00646

OSTI ID:: 1562698

Journal Information:: FEBS Open Bio, Vol. 9, Issue 9; ISSN 2211-5463

Publisher:: Federation of European Biochemical SocietiesCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 13 works

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59 BASIC BIOLOGICAL SCIENCES
AAA+ proteins
ATPase module
ClpB chaperones
coiled-coil fragments
inserted a-helical domain
Lon protease

Title: New insights into structural and functional relationships between LonA proteases and ClpB chaperones

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