scholarly journals Multiple shifts between violet and ultraviolet vision in a family of passerine birds with associated changes in plumage coloration

2011 ◽  
Vol 279 (1732) ◽  
pp. 1269-1276 ◽  
Author(s):  
Anders Ödeen ◽  
Stephen Pruett-Jones ◽  
Amy C. Driskell ◽  
Jessica K. Armenta ◽  
Olle Håstad
Keyword(s):  
Plumage Coloration ◽  
Amino Acid Residues ◽  
Avian Evolution ◽  
Phylogenetic Reconstructions ◽  
Single Cone ◽  
Male Plumage ◽  
Ultraviolet Vision ◽  
Character Correlation ◽  
Cone Opsins

Colour vision in diurnal birds falls into two discrete classes, signified by the spectral sensitivity of the violet- (VS) or ultraviolet-sensitive (UVS) short wavelength-sensitive type 1 (SWS1) single cone. Shifts between sensitivity classes are rare; three or four are believed to have happened in the course of avian evolution, one forming UVS higher passerines. Such shifts probably affect the expression of shortwave-dominated plumage signals. We have used genomic DNA sequencing to determine VS or UVS affinity in fairy-wrens and allies, Maluridae, a large passerine family basal to the known UVS taxa. We have also spectrophotometrically analysed male plumage coloration as perceived by the VS and UVS vision systems. Contrary to any other investigated avian genus, Malurus (fairy-wrens) contains species with amino acid residues typical of either VS or UVS cone opsins. Three bowerbird species (Ptilonorhynchidae) sequenced for outgroup comparison carry VS opsin genes. Phylogenetic reconstructions render one UVS gain followed by one or more losses as the most plausible evolutionary scenario. The evolution of avian ultraviolet sensitivity is hence more complex, as a single shift no longer explains its distribution in Passeriformes. Character correlation analysis proposes that UVS vision is associated with shortwave-reflecting plumage, which is widespread in Maluridae.

scholarly journals The Structural Characterization and Antipathogenic Activities of Quinoin, a Type 1 Ribosome-Inactivating Protein from Quinoa Seeds

2021 ◽  
Vol 22 (16) ◽  
pp. 8964
Author(s):  
Sara Ragucci ◽  
Daniela Bulgari ◽  
Nicola Landi ◽  
Rosita Russo ◽  
Angela Clemente ◽  
...  
Keyword(s):  
Amino Acid ◽  
Homology Modeling ◽  
Peptide Mapping ◽  
Cryphonectria Parasitica ◽  
Tobacco Necrosis Virus ◽  
Amino Acid Residues ◽  
Ribosome Inactivating Protein ◽  
Defensive Role

Quinoin is a type 1 ribosome-inactivating protein (RIP) we previously isolated from the seeds of pseudocereal quinoa (Chenopodium quinoa) and is known as a functional food for its beneficial effects on human health. As the presence of RIPs in edible plants could be potentially risky, here we further characterised biochemically the protein (complete amino acid sequence, homologies/differences with other RIPs and three-dimensional homology modeling) and explored its possible defensive role against pathogens. Quinoin consists of 254 amino acid residues, without cysteinyl residues. As demonstrated by similarities and homology modeling, quinoin preserves the amino acid residues of the active site (Tyr75, Tyr122, Glu177, Arg180, Phe181 and Trp206; quinoin numbering) and the RIP-fold characteristic of RIPs. The polypeptide chain of quinoin contains two N-glycosylation sites at Asn115 and Asp231, the second of which appears to be linked to sugars. Moreover, by comparative MALDI-TOF tryptic peptide mapping, two differently glycosylated forms of quinoin, named pre-quinoin-1 and pre-quinoin-2 (~0.11 mg/100 g and ~0.85 mg/100 g of seeds, respectively) were characterised. Finally, quinoin possesses: (i) strong antiviral activity, both in vitro and in vivo towards Tobacco Necrosis Virus (TNV); (ii) a growth inhibition effect on the bacterial pathogens of plants; and (iii) a slight antifungal effect against two Cryphonectria parasitica strains.

scholarly journals Amino Acid Residues Gln4020and Lys4021of the Ryanodine Receptor Type 1 Are Required for Activation by 4-Chloro-m-cresol

2006 ◽  
Vol 281 (30) ◽  
pp. 21022-21031 ◽  
Author(s):  
James D. Fessenden ◽  
Wei Feng ◽  
Isaac N. Pessah ◽  
Paul D. Allen
Keyword(s):  
Amino Acid ◽  
Ryanodine Receptor ◽  
Receptor Type ◽  
Amino Acid Residues

scholarly journals Next-Generation HLA Sequence Analysis Uncovers Seven HLA-DQ Amino Acid Residues and Six Motifs Resistant to Childhood Type 1 Diabetes

Diabetes ◽  
2020 ◽  
Vol 69 (11) ◽  
pp. 2523-2535
Author(s):  
Lue Ping Zhao ◽  
George K. Papadopoulos ◽  
William W. Kwok ◽  
Antonis K. Moustakas ◽  
George P. Bondinas ◽  
...  
Keyword(s):  
Type 1 Diabetes ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Residues ◽  
Next Generation ◽  
Hla Dq ◽  
Childhood Type 1 Diabetes ◽  
Childhood Type

scholarly journals Novel LinA Type 3 δ-Hexachlorocyclohexane Dehydrochlorinase

2015 ◽  
Vol 81 (21) ◽  
pp. 7553-7559 ◽  
Author(s):  
Nidhi Shrivastava ◽  
Zbynek Prokop ◽  
Ashwani Kumar
Keyword(s):  
Amino Acid ◽  
Primary Structure ◽  
Degradation Pathway ◽  
Amino Acid Residues ◽  
Hch Isomers ◽  
New Variant ◽  
Type 3

ABSTRACTLinA is the first enzyme of the microbial degradation pathway of a chlorinated insecticide, hexachlorocyclohexane (HCH), and mediates the dehydrochlorination of α-, γ-, and δ-HCH. Its two variants, LinA type 1 and LinA type 2, which differ at 10 out of 156 amino acid residues, have been described. Their activities for the metabolism of different HCH isomers differ considerably but overall are high for γ-HCH, moderate for α-HCH, low for δ-HCH, and lacking for β-HCH. Here, we describe the characterization of a new variant of this enzyme, LinA type 3, whose gene was identified from the metagenome of an HCH-contaminated soil sample. Its deduced primary structure in the region spanning amino acid residues 1 to 147 of the protein exhibits 17 and 12 differences from LinA type 1 and LinA type 2, respectively. In addition, the residues GIHFAPS, present at the region spanning residues 148 to 154 in both LinA type 1 and LinA type 2, are deleted in LinA type 3.The activity of LinA type 3 for the metabolism of δ-HCH is several orders of magnitude higher than that of LinA type 1 or LinA type 2 and can be useful for improvement of the metabolism of δ-HCH.

scholarly journals In silico prediction of the functional and structural consequences of the non-synonymous single nucleotide polymorphism A122V in bovine CXC chemokine receptor type 1

2020 ◽  
Vol 80 (1) ◽  
pp. 39-46
Author(s):  
A. F. Guzzi ◽  
F. S. L. Oliveira ◽  
M. M. S. Amaro ◽  
P. F. Tavares-Filho ◽  
J. E. Gabriel
Keyword(s):  
Amino Acid ◽  
Chemokine Receptor ◽  
In Silico ◽  
Alpha Helix ◽  
Amino Acid Sequences ◽  
Receptor Type ◽  
Amino Acid Residues ◽  
Causal Polymorphism ◽  
Cxc Chemokine

Abstract The current study aimed to assess whether the A122V causal polymorphism promotes alterations in the functional and structural proprieties of the CXC chemokine receptor type 1 protein (CXCR1) of cattle Bos taurus by in silico analyses. Two amino acid sequences of bovine CXCR1 was selected from database UniProtKB/Swiss-Prot: a) non-polymorphic sequence (A7KWG0) with alanine (A) at position 122, and b) polymorphic sequence harboring the A122V polymorphism, substituting alanine by valine (V) at same position. CXCR1 sequences were submitted as input to different Bioinformatics’ tools to examine the effects of this polymorphism on functional and structural stabilities, to predict eventual alterations in the 3-D structural modeling, and to estimate the quality and accuracy of the predictive models. The A122V polymorphism exerted tolerable and non-deleterious effects on the polymorphic CXCR1, and the predictive structural model for polymorphic CXCR1 revealed an alpha helix spatial structure typical of a receptor transmembrane polypeptide. Although higher variations in the distances between pairs of amino acid residues at target-positions are detected in the polymorphic CXCR1 protein, more than 97% of the amino acid residues in both models were located in favored and allowed conformational regions in Ramachandran plots. Evidences has supported that the A122V polymorphism in the CXCR1 protein is associated with increased clinical mastitis incidence in dairy cows. Thus, the findings described herein prove that the replacement of the alanine by valine amino acids provokes local conformational changes in the A122V-harboring CXCR1 protein, which could directly affect its post-translational folding mechanisms and biological functionality.

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