: Proteorhodopsins are widely distributed photoreceptors from marine bacteria. Their discovery revealed a high degree of evolutionary adaptation to ambient light, resulting in blue- and green-absorbing variants that correlate with a conserved glutamine/leucine at position 105. On the basis of an integrated approach combining sensitivity-enhanced solid-state nuclear magnetic resonance (ssNMR) spectroscopy and linear-scaling quantum mechanics/molecular mechanics (QM/MM) methods, this single residue is shown to be responsible for a variety of synergistically coupled structural and electrostatic changes along the retinal polyene chain, ionone ring, and within the binding pocket. They collectively explain the observed color shift. Furthermore, analysis of the differences in chemical shift between nuclei within the same residues in green and blue proteorhodopsins also reveals a correlation with the respective degree of conservation. Our data show that the highly conserved color change mainly affects other highly conserved residues, illustrating a high degree of robustness of the color phenotype to sequence variation.

Molecular mechanisms and evolutionary robustness of a color switch in proteorhodopsins / Jiafei Mao; Xinsheng Jin; Man Shi; David Heidenreich; Lynda J. Brown; Richard C. D. Brown; Moreno Lelli; Xiao He; Clemens Glaubitz. - In: SCIENCE ADVANCES. - ISSN 2375-2548. - STAMPA. - 10:(2024), pp. eadj0384-eadj0384. [10.1126/sciadv.adj0384]

Molecular mechanisms and evolutionary robustness of a color switch in proteorhodopsins

Jiafei Mao
;
Moreno Lelli;
2024

Abstract

: Proteorhodopsins are widely distributed photoreceptors from marine bacteria. Their discovery revealed a high degree of evolutionary adaptation to ambient light, resulting in blue- and green-absorbing variants that correlate with a conserved glutamine/leucine at position 105. On the basis of an integrated approach combining sensitivity-enhanced solid-state nuclear magnetic resonance (ssNMR) spectroscopy and linear-scaling quantum mechanics/molecular mechanics (QM/MM) methods, this single residue is shown to be responsible for a variety of synergistically coupled structural and electrostatic changes along the retinal polyene chain, ionone ring, and within the binding pocket. They collectively explain the observed color shift. Furthermore, analysis of the differences in chemical shift between nuclei within the same residues in green and blue proteorhodopsins also reveals a correlation with the respective degree of conservation. Our data show that the highly conserved color change mainly affects other highly conserved residues, illustrating a high degree of robustness of the color phenotype to sequence variation.
2024
10
eadj0384
eadj0384
Goal 3: Good health and well-being
Jiafei Mao; Xinsheng Jin; Man Shi; David Heidenreich; Lynda J. Brown; Richard C. D. Brown; Moreno Lelli; Xiao He; Clemens Glaubitz
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1352731
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