E. coli metabolic protein aldehyde-alcohol dehydrogenase-E binds to the ribosome: a unique moonlighting action revealed

Scientific Reports
Manidip ShasmalJayati Sengupta

Abstract

It is becoming increasingly evident that a high degree of regulation is involved in the protein synthesis machinery entailing more interacting regulatory factors. A multitude of proteins have been identified recently which show regulatory function upon binding to the ribosome. Here, we identify tight association of a metabolic protein aldehyde-alcohol dehydrogenase E (AdhE) with the E. coli 70S ribosome isolated from cell extract under low salt wash conditions. Cryo-EM reconstruction of the ribosome sample allows us to localize its position on the head of the small subunit, near the mRNA entrance. Our study demonstrates substantial RNA unwinding activity of AdhE which can account for the ability of ribosome to translate through downstream of at least certain mRNA helices. Thus far, in E. coli, no ribosome-associated factor has been identified that shows downstream mRNA helicase activity. Additionally, the cryo-EM map reveals interaction of another extracellular protein, outer membrane protein C (OmpC), with the ribosome at the peripheral solvent side of the 50S subunit. Our result also provides important insight into plausible functional role of OmpC upon ribosome binding. Visualization of the ribosome purified directly from th...Continue Reading

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Citations

Sep 12, 2017·Nature Ecology & Evolution·Michael J BotteryMichael A Brockhurst
Jan 9, 2021·Plant Molecular Biology·Robert van LisAriane Atteia
Aug 19, 2017·International Journal of Biological Macromolecules·Pankaj SharmaBishwajit Kundu

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Datasets Mentioned

BETA
EMD-2972

Methods Mentioned

BETA
electrophoresis
helicase
helicase assay
X-ray

Software Mentioned

ResMap
PyMol
MASCOT
PHYRE2
NSitePred
ImageJ
MDFF
SPIDER
Adaptive Poisson Boltzmann Solver ( APBS )

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