Mechanisms of protein evolution

V Jayaraman, S Toledo‐Patiño, L Noda‐García… - Protein …, 2022 - Wiley Online Library
How do proteins evolve? How do changes in sequence mediate changes in protein
structure, and in turn in function? This question has multiple angles, ranging from …

[HTML][HTML] Impact of the resistance responses to stress conditions encountered in food and food processing environments on the virulence and growth fitness of non …

S Guillén, L Nadal, I Álvarez, P Mañas, G Cebrián - Foods, 2021 - mdpi.com
The success of Salmonella as a foodborne pathogen can probably be attributed to two major
features: its remarkable genetic diversity and its extraordinary ability to adapt. Salmonella …

Potential and active functions in the gut microbiota of a healthy human cohort

A Tanca, M Abbondio, A Palomba, C Fraumene… - Microbiome, 2017 - Springer
Background The study of the gut microbiota (GM) is rapidly moving towards its functional
characterization by means of shotgun meta-omics. In this context, there is still no consensus …

Viral evolution shaped by host proteostasis networks

J Yoon, JE Patrick, CB Ogbunugafor… - Annual review of …, 2023 - annualreviews.org
Understanding the factors that shape viral evolution is critical for develo** effective
antiviral strategies, accurately predicting viral evolution, and preventing pandemics. One …

Dissecting genome reduction and trait loss in insect endosymbionts

A Latorre, A Manzano‐Marín - … of the New York Academy of …, 2017 - Wiley Online Library
Symbiosis has played a major role in eukaryotic evolution beyond the origin of the
eukaryotic cell. Thus, organisms across the tree of life are associated with diverse microbial …

Selection transforms the landscape of genetic variation interacting with Hsp90

KA Geiler-Samerotte, YO Zhu, BE Goulet, DW Hall… - PLoS …, 2016 - journals.plos.org
The protein-folding chaperone Hsp90 has been proposed to buffer the phenotypic effects of
mutations. The potential for Hsp90 and other putative buffers to increase robustness to …

The molecular chaperone DnaK is a source of mutational robustness

J Aguilar-Rodríguez, B Sabater-Munoz… - Genome biology and …, 2016 - academic.oup.com
Molecular chaperones, also known as heat-shock proteins, refold misfolded proteins and
help other proteins reach their native conformation. Thanks to these abilities, some …

Evolution of drift robustness in small populations

T LaBar, C Adami - Nature Communications, 2017 - nature.com
Most mutations are deleterious and cause a reduction in population fitness known as the
mutational load. In small populations, weakened selection against slightly-deleterious …

Elevated temperature increases genome-wide selection on de novo mutations

D Berger, J Stångberg, J Baur… - Proceedings of the …, 2021 - royalsocietypublishing.org
Adaptation in new environments depends on the amount of genetic variation available for
evolution, and the efficacy by which natural selection discriminates among this variation …

[PDF][PDF] GroEL/S overexpression helps to purge deleterious mutations and reduce genetic diversity during adaptive protein evolution

BR Iyengar, A Wagner - Molecular Biology and Evolution, 2022 - academic.oup.com
Chaperones are proteins that help other proteins fold. They also affect the adaptive
evolution of their client proteins by buffering the effect of deleterious mutations and …