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PreprintCited by 9Bacterial Genetics and BiotechnologyATP Synthase and ATPases ResearchProtein Structure and Dynamics

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Ancestral reconstruction of the MotA stator subunit reveals that conserved residues far from the pore are required to drive flagellar motility

Open access
Islam, Md Imtiazul, Ridone, Pietro, Lin, Angela, Michie, Katharine A, Matzke, Nicholas J, Hochberg, Georg, Baker, Matthew AB·2022·microLife
DOI 10.1101/2022.10.17.512626PMC PMC10117855

Preprint — published as 10.1093/femsml/uqad011 · Paper page

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Abstract

The bacterial flagellar motor (BFM) is a rotary nanomachine powered by the translocation of ions across the inner membrane through the stator complex. The stator complex consists of two membrane proteins: MotA and MotB (in H + powered motors), or PomA and PomB (in Na + powered motors). In this study we used ancestral sequence reconstruction (ASR) to probe which residues of MotA correlate with function and may have been conserved to preserve motor function. We reconstructed ten ancestral sequences of MotA and found four of them were motile in combination with contemporary E. coli MotB and in combination with our previously published functional ancestral MotBs. Sequence comparison between wild-type (WT) E. coli MotA and MotA-ASRs revealed 30 critical residues across multiple domains of MotA that were conserved among all motile stator units. These conserved residues included pore-facing, cytoplasm-facing and MotA-MotA intermolecular facing sites. Overall, this work demonstrates the role of ASR in assessing conserved variable residues in a subunit of a molecular complex.

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Metadata

Authors
Islam, M. I., Ridone, P., Lin, A., Michie, K. A., Matzke, N. J., Hochberg, G., & Baker, M. A.
Affiliations
  • UNSW Sydney (AU)
  • University of Auckland (NZ)
  • Philipps University of Marburg (DE)
Corresponding author
Baker, Matthew AB
ORCID
Venue
microLife
Publisher
openRxiv
Published
2022-10-18
Volume
4
Pages
uqad011-uqad011
ISSN
2633-6693 (ISSN-L)
DOI
10.1101/2022.10.17.512626
PMC
PMC10117855
OpenAlex
W4362568821
Cited by
9
References
1
Citations by year
2026: 1 · 2025: 2 · 2024: 3 · 2023: 3
FWCI
1.49
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • microLife (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • ResearchSpace (University of Auckland) (submittedVersion, cc-by)
Funders
  • Human Frontier Science Program
  • Analytical Center for the Government of the Russian Federation
  • Commonwealth Scientific and Industrial Research Organisation
  • University of New South Wales
  • Australian Research Council (DP190100497, ARC LIEF 190100165, 190100165)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
flagellar motor, MotB, ancestral sequence reconstruction, conserved residues, flagellar motility, Escherichia coli, ion translocation

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