Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pbio.2004920
Title: Evolutionary novelty in gravity sensing through horizontal gene transfer and high-order protein assembly
Authors: Nguyen T.A.
Greig J.
Khan A. 
Goh C.
Jedd G. 
Keywords: bacterial protein
octahedral crystal matrix protein
oligomer
unclassified drug
bacterial protein
green fluorescent protein
photoprotein
recombinant protein
red fluorescent protein
amino terminal sequence
Article
bacterial structures
carboxy terminal sequence
controlled study
gene
gravity sensing
horizontal gene transfer
human
human cell
mass spectrometry
molecular evolution
molecular imaging
nonhuman
octin gene
Phycomyces blakesleeanus
phylogeny
protein analysis
protein assembly
protein expression
protein localization
protein structure
cell vacuole
chemistry
classification
Escherichia coli
evolution
gene expression
gene vector
genetics
gravity
HeLa cell line
metabolism
molecular cloning
Mucorales
periplasm
protein multimerization
reporter gene
Bacterial Proteins
Biological Evolution
Cloning, Molecular
Escherichia coli
Gene Expression
Gene Transfer, Horizontal
Genes, Reporter
Genetic Vectors
Gravitation
Green Fluorescent Proteins
HeLa Cells
Humans
Luminescent Proteins
Mucorales
Periplasm
Phylogeny
Protein Multimerization
Recombinant Proteins
Vacuoles
Issue Date: 2018
Publisher: Public Library of Science
Citation: Nguyen T.A., Greig J., Khan A., Goh C., Jedd G. (2018). Evolutionary novelty in gravity sensing through horizontal gene transfer and high-order protein assembly. PLoS Biology 16 (4) : e2004920. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pbio.2004920
Abstract: Horizontal gene transfer (HGT) can promote evolutionary adaptation by transforming a species' relationship to the environment. In most well-understood cases of HGT, acquired and donor functions appear to remain closely related. Thus, the degree to which HGT can lead to evolutionary novelties remains unclear. Mucorales fungi sense gravity through the sedimentation of vacuolar protein crystals. Here, we identify the octahedral crystal matrix protein (OCTIN). Phylogenetic analysis strongly supports acquisition of octin by HGT from bacteria. A bacterial OCTIN forms high-order periplasmic oligomers, and inter-molecular disulphide bonds are formed by both fungal and bacterial OCTINs, suggesting that they share elements of a conserved assembly mechanism. However, estimated sedimentation velocities preclude a gravity-sensing function for the bacterial structures. Together, our data suggest that HGT from bacteria into the Mucorales allowed a dramatic increase in assembly scale and emergence of the gravity-sensing function. We conclude that HGT can lead to evolutionary novelties that emerge depending on the physiological and cellular context of protein assembly. © 2018 Nguyen et al.
Source Title: PLoS Biology
URI: https://scholarbank.nus.edu.sg/handle/10635/165619
ISSN: 15449173
DOI: 10.1371/journal.pbio.2004920
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