Studies in vitamin A. 11. Reactions of retinene1 with amino compounds

Ball, S.; Collins, F. D.; Dalvi, Pooja; Morton, R. A.

doi:10.1042/bj0450304

Cited by 85 publications

(31 citation statements)

References 1 publication

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Interacting with an opsin, however, the Schiff base-linked chromophore in a visual pigment can have a l max from 360 to 635 nm (Kochendoerfer et al, 1999). On the other hand, the unprotonated Schiff base-linked chromophore in solution has a l max of 365 nm (Ball et al, 1949).…”

Section: Discussionmentioning

confidence: 99%

Molecular evolution of color vision in vertebrates

Yokoyama

2002

Gene

261

231

View full text Add to dashboard Cite

Visual systems of vertebrates exhibit a striking level of diversity, reflecting their adaptive responses to various color environments. The photosensitive molecules, visual pigments, can be synthesized in vitro and their absorption spectra can be determined. Comparing the amino acid sequences and absorption spectra of various visual pigments, we can identify amino acid changes that have modified the absorption spectra of visual pigments. These hypotheses can then be tested using the in vitro assay. This approach has been a powerful tool in elucidating not only the molecular bases of color vision, but the processes of adaptive evolution at the molecular level. q

show abstract

Section: Discussionmentioning

confidence: 99%

Molecular evolution of color vision in vertebrates

Yokoyama

2002

Gene

261

231

View full text Add to dashboard Cite

show abstract

“…The chromophore 11- cis -retinal in solution has a λ max of 440 nm in its protonated form (1) and 365 nm in the unprotonated form (2). However, by interacting with various short wavelength-sensitive type 1 (SWS1) opsins, the retinals achieve a diverse range of λ max s between 360 and 440 nm (3).…”

mentioning

confidence: 99%

H-Bond Network around Retinal Regulates the Evolution of Ultraviolet and Violet Vision

2011

View full text Add to dashboard Cite

Ancestors of vertebrates used ultraviolet vision. Some descendants preserved ultraviolet vision while some others replaced it with violet vision, and then, some of avian lineages reinvented ultraviolet vision. Ultraviolet (absorption at ~360 nm) and violet (410–440 nm) sensitivities of visual pigments are known to be affected by around 20 amino acid substitutions. The present quantum mechanical/molecular mechanical calculations show that these substitutions modify a H-bond network formed by two waters and sites 86, 90, 113, 114, 118 and 295, which determines the protonation state of Schiff base-linked 11-cis-retinal. A pigment is ultraviolet-sensitive when it is more stable with an unprotonated retinal (SBR) form than with its protonated analog (PSBR), and is violet-sensitive when the PSBR form is more stable. These results establish for the first time the chemical basis of ultraviolet and violet vision in vertebrates.

show abstract

“…Through the interaction with an opsin, however, the Schiff base-linked chromophore in a visual pigment can have a max ranging from 360 to 635 nm (11). Interestingly, the unprotonated Schiff base-linked chromophore in solution has a max at 365 nm (12). Thus, it has been proposed that UV pigments may have an unprotonated Schiff base-linked chromophore (13)(14)(15)(16)(17), but this hypothesis has not been experimentally tested.…”

mentioning

confidence: 99%

Molecular genetics and the evolution of ultraviolet vision in vertebrates

Shi

Radlwimmer²,

Yokoyama³

2001

Proc. Natl. Acad. Sci. U.S.A.

146

227

View full text Add to dashboard Cite

Despite the biological importance of UV vision, its molecular bases are not well understood. Here, we present evidence that UV vision in vertebrates is determined by eight specific amino acids in the UV pigments. Amino acid sequence analyses show that contemporary UV pigments inherited their UV sensitivities from the vertebrate ancestor by retaining most of these eight amino acids. In the avian lineage, the ancestral pigment lost UV sensitivity, but some descendants regained it by one amino acid change. Our results also strongly support the hypothesis that UV pigments have an unprotonated Schiff base-linked chromophore. It is now clear that, counter to the traditional view, many vertebrates use UV vision for such basic behaviors as foraging, social signaling, and mating (1-5). UV vision is achieved by the pigments that absorb light maximally ( max ) at Ϸ360 nm, but the mechanisms of the spectral tuning in these UV pigments remain mostly as an area of speculation. In general, visual pigments consist of an apoprotein, opsin, and an 11-cis-retinal chromophore that is bound to opsin by a Schiff base linkage to the lysine residue in the center of the seventh transmembrane (TM) helix (6). The Schiff base of 11-cis-retinal is usually protonated by the glutamate counterion in the third TM helix (7-9). The protonated Schiff base has a max at 440 nm in solution (10). Through the interaction with an opsin, however, the Schiff base-linked chromophore in a visual pigment can have a max ranging from 360 to 635 nm (11). Interestingly, the unprotonated Schiff base-linked chromophore in solution has a max at 365 nm (12). Thus, it has been proposed that UV pigments may have an unprotonated Schiff base-linked chromophore (13-17), but this hypothesis has not been experimentally tested.Recently, it has been shown that some avian species have acquired UV vision by one amino acid change (17,18). It is also proposed that five amino acid sites regulate the absorption spectra of UV pigments in nonavian species (19). This evolutionary approach, however, lacks rigor in identifying all amino acids involved in the spectral tuning in the UV pigments. Here, to study the molecular bases of UV vision, we first determine the mechanisms of the spectral tuning in the mouse UV pigment. The general molecular bases of UV vision in vertebrates are then studied by considering the mouse UV pigment and other orthologous pigments, often referred to as short-wavelengthsensitive type 1 (SWS1) pigments (20,21). Using the mouse UV pigment, we also examine the effects of the glutamate counterion on the spectral sensitivities of visual pigments. Materials and Methods Construction of Chimeric Pigments and Site-Directed Mutagenesis.The UV opsin cDNA clone of the mouse (Mus musculus) has been subcloned into an expression vector, pMT5 (22). The human blue opsin cDNA clone is a gift from Jeremy Nathans (Johns Hopkins Univ., Baltimore). To subclone the human blue opsin cDNA into pMT5, the cDNA clone was amplified by PCR by using primers: 5Ј-AGGGTGGAATTCCACCATG-AGAAAAA...

show abstract

Studies in vitamin A. 11. Reactions of retinene1 with amino compounds

Cited by 85 publications

References 1 publication

Molecular evolution of color vision in vertebrates

Molecular evolution of color vision in vertebrates

H-Bond Network around Retinal Regulates the Evolution of Ultraviolet and Violet Vision

Molecular genetics and the evolution of ultraviolet vision in vertebrates

Contact Info

Product

Resources

About