Protein Structure: Systematic Alteration of Amino Acid Sequences

Science ◽  
1976 ◽  
Vol 191 (4225) ◽  
pp. 373-373 ◽  
Author(s):  
G. B. KOLATA
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
Amino Acid Sequences

scholarly journals Intergenic ORFs as elementary structural modules of de novo gene birth and protein evolution

2021 ◽  
Author(s):  
Chris Papadopoulos ◽  
Isabelle Callebaut ◽  
Jean-Christophe Gelly ◽  
Isabelle Hatin ◽  
Olivier Namy ◽  
...  
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
De Novo ◽  
Protein Structures ◽  
Structural Diversity ◽  
Building Blocks ◽  
Amino Acid Sequences ◽  
Novel Genes ◽  
Noncoding Sequences ◽  
De Novo Gene

The noncoding genome plays an important role in de novo gene birth and in the emergence of genetic novelty. Nevertheless, how noncoding sequences' properties could promote the birth of novel genes and shape the evolution and the structural diversity of proteins remains unclear. Therefore, by combining different bioinformatic approaches, we characterized the fold potential diversity of the amino acid sequences encoded by all intergenic ORFs (Open Reading Frames) of S. cerevisiae with the aim of (i) exploring whether the large structural diversity observed in proteomes is already present in noncoding sequences, and (ii) estimating the potential of the noncoding genome to produce novel protein bricks that can either give rise to novel genes or be integrated into pre-existing proteins, thus participating in protein structure diversity and evolution. We showed that amino acid sequences encoded by most yeast intergenic ORFs contain the elementary building blocks of protein structures. Moreover, they encompass the large structural diversity of canonical proteins with strikingly the majority predicted as foldable. Then, we investigated the early stages of de novo gene birth by identifying intergenic ORFs with a strong translation signal in ribosome profiling experiments and by reconstructing the ancestral sequences of 70 yeast de novo genes. This enabled us to highlight sequence and structural factors determining de novo gene emergence. Finally, we showed a strong correlation between the fold potential of de novo proteins and the one of their ancestral amino acid sequences, reflecting the relationship between the noncoding genome and the protein structure universe.

scholarly journals Dye Decoloring Peroxidase Structure, Catalytic Properties and Applications: Current Advancement and Futurity

Catalysts ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 955
Author(s):  
Lingxia Xu ◽  
Jianzhong Sun ◽  
Majjid A. Qaria ◽  
Lu Gao ◽  
Daochen Zhu
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
High Efficiency ◽  
Chemical Properties ◽  
Catalytic Efficiency ◽  
Industrial Applications ◽  
Research Strategy ◽  
Amino Acid Sequences ◽  
Alkali Resistance ◽  
Wide Range

Dye decoloring peroxidases (DyPs) were named after their high efficiency to decolorize and degrade a wide range of dyes. DyPs are a type of heme peroxidase and are quite different from known heme peroxidases in terms of amino acid sequences, protein structure, catalytic residues, and physical and chemical properties. DyPs oxidize polycyclic dyes and phenolic compounds. Thus they find high application potentials in dealing with environmental problems. The structure and catalytic characteristics of DyPs of different families from the amino acid sequence, protein structure, and enzymatic properties, and analyzes the high-efficiency degradation ability of some DyPs in dye and lignin degradation, which vary greatly among DyPs classes. In addition, application prospects of DyPs in biomedicine and other fields are also discussed briefly. At the same time, the research strategy based on genetic engineering and synthetic biology in improving the stability and catalytic activity of DyPs are summarized along with the important industrial applications of DyPs and associated challenges. Moreover, according to the current research findings, bringing DyPs to the industrial level may require improving the catalytic efficiency of DyP, increasing production, and enhancing alkali resistance and toxicity.

scholarly journals Oxidant-Mediated Protein Amino Acid Conversion

Antioxidants ◽  
2019 ◽  
Vol 8 (2) ◽  
pp. 50 ◽  
Author(s):  
Yuichiro Suzuki
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
Biological System ◽  
Redox Regulation ◽  
Amino Acid Sequences ◽  
Biological Oxidation ◽  
Oxidation Reactions ◽  
Protein Amino Acid ◽  
Peroxiredoxin 6 ◽  
Protein Molecules

Biological oxidation plays important roles in the pathogenesis of various diseases and aging. Carbonylation is one mode of protein oxidation. It has been reported that amino acids that are susceptible to carbonylation are arginine (Arg), proline (Pro), lysine, and threonine residues. The carbonylation product of both Arg and Pro residues is glutamyl semialdehyde. While chemically the oxidation reactions of neither Pro to glutamyl semialdehyde nor Arg to glutamyl semialdehyde are reversible, experimental results from our laboratory suggest that the biological system may drive the reduction of glutamyl semialdehyde to Pro in the protein structure. Further, glutamyl semialdehyde can be oxidized to become glutamic acid (Glu). Therefore, I hypothesize that biological oxidation post-translationally converts Arg to Pro, Arg to Glu, and Pro to Glu within the protein structure. Our mass spectrometry experiments provided evidence that, in human cells, 5–10% of peroxiredoxin 6 protein molecules have Pro-45 replaced by Glu. This concept of protein amino acid conversion challenges the dogma that amino acid sequences are strictly defined by nucleic acid sequences. I propose that, in the biological system, amino acid replacements can occur post-translationally through redox regulation, and protein molecules with non-DNA coding sequences confer functions.

scholarly journals Amino acid torsion angles enable prediction of protein fold classification

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Kun Tian ◽  
Xin Zhao ◽  
Xiaogeng Wan ◽  
Stephen S.-T. Yau
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
Protein Structure Prediction ◽  
Structure Prediction ◽  
High Throughput Sequencing ◽  
Protein Structures ◽  
Amino Acid Sequences ◽  
Single Amino Acid ◽  
New Approach ◽  
Protein Functions

AbstractProtein structure can provide insights that help biologists to predict and understand protein functions and interactions. However, the number of known protein structures has not kept pace with the number of protein sequences determined by high-throughput sequencing. Current techniques used to determine the structure of proteins are complex and require a lot of time to analyze the experimental results, especially for large protein molecules. The limitations of these methods have motivated us to create a new approach for protein structure prediction. Here we describe a new approach to predict of protein structures and structure classes from amino acid sequences. Our prediction model performs well in comparison with previous methods when applied to the structural classification of two CATH datasets with more than 5000 protein domains. The average accuracy is 92.5% for structure classification, which is higher than that of previous research. We also used our model to predict four known protein structures with a single amino acid sequence, while many other existing methods could only obtain one possible structure for a given sequence. The results show that our method provides a new effective and reliable tool for protein structure prediction research.

scholarly journals Seven SNPs in the Coding Sequence of Leptin Receptor Gene in Long-term Selected Japanese Quail Lines

2016 ◽  
Author(s):  
Kemal Karabağ ◽  
Sezai Alkan ◽  
Taki Karslı ◽  
Cengiz İkten ◽  
İnci Sahin ◽  
...  
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
Leptin Receptor ◽  
Receptor Gene ◽  
Amino Acid Sequences ◽  
Phenotypic Traits ◽  
Coding Region ◽  
Coding Sequence ◽  
Secondary Protein Structure

The objective of this study was to identify SNPs in the coding sequence of the leptin receptor gene and to test for their possible association with 20 economically advantageous traits in 15 generations of 2 selected (HBW and LBW) and a control of japanase quail. A 350-bp part of the leptin receptor coding region was amplified and sequenced and understood that the fragment contained 7 SNPs (GenBank:KP674322.1-KP674328.1) that were detected in 5 loci (T3216C, T3265C, T3265G, C3265G, T3303C, A3311G, and T3347C) in a total of 30 individuals. The T3216C and T3303C SNPs located at the end of the codon were synonymous and did not affect the presence of proline. However, phenylalanine, leucine and valine were produced when the T3265C, T3265G and C3265G SNPs, respectively, were present. Glutamine or arginine was produced when the A3311G SNP was A or G, respectively, and serine was produced when the T3347C SNP was C. Although codons and amino acid sequences changed due to the second SNP, the secondary protein structure was not changed. However, the fourth and fifth SNPs changed both the amino acid sequences and secondary protein structure. Pairing the SNP loci with phenotypic traits created haplogroups. When all individuals were evaluated together, some of the differences between the haplogroups were statistically significant (p<0.05; p<0.01). These results showed that both the sequence and structure of the leptin receptor gene could be altered by long-term selection. However, to achieve a more precise understanding of the role of leptin, entire coding sequences of leptin and the leptin receptor should be studied.

scholarly journals A divergent Articulavirus in an Australian gecko identified using meta-transcriptomics and protein structure comparisons

2020 ◽  
Author(s):  
Ayda Susana Ortiz-Baez ◽  
John-Sebastian Eden ◽  
Craig Moritz ◽  
Edward C. Holmes
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
Protein Structure Prediction ◽  
Structure Prediction ◽  
Rna Viruses ◽  
Sequence Data ◽  
Gene Segment ◽  
Amino Acid Sequences ◽  
Evolutionary Information ◽  
Negative Sense

AbstractThe discovery of highly divergent RNA viruses is compromised by their limited sequence similarity to known viruses. Evolutionary information obtained from protein structural modelling offers a powerful approach to detect distantly related viruses based on the conservation of tertiary structures in key proteins such as the viral RNA-dependent RNA polymerase (RdRp). We utilised a template-based approach for protein structure prediction from amino acid sequences to identify distant evolutionary relationships among viruses detected in meta-transcriptomic sequencing data from Australian wildlife. The best predicted protein structural model was compared with the results of similarity searches against protein databases based on amino acid sequence data. Using this combination of meta-transcriptomics and protein structure prediction we identified the RdRp (PB1) gene segment of a divergent negative-sense RNA virus in a native Australian gecko (Geyra lauta) that was confirmed by PCR and Sanger sequencing. Phylogenetic analysis identified the Gecko articulavirus (GECV) as a newly described genus within the family Amnoonviridae, order Articulavirales, that is most closely related to the fish virus Tilapia tilapinevirus (TiLV). These findings provide important insights into the evolution of negative-sense RNA viruses and structural conservation of the viral replicase among members of the order Articulavirales.

scholarly journals Intergenic ORFs as elementary structural modules of de novo gene birth and protein evolution

2021 ◽  
Author(s):  
Chris Papadopoulos ◽  
Isabelle Callebaut ◽  
Jean-Christophe Gelly ◽  
Isabelle Hatin ◽  
Olivier Namy ◽  
...  
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
De Novo ◽  
Protein Structures ◽  
Building Blocks ◽  
Amino Acid Sequences ◽  
Novel Genes ◽  
Noncoding Sequences ◽  
Ancestral Sequences ◽  
De Novo Gene

The noncoding genome plays an important role in de novo gene birth and in the emergence of genetic novelty. Nevertheless, how noncoding sequences’ properties could promote the birth of novel genes and shape the evolution and the structural diversity of proteins remains unclear. Therefore, by combining different bioinformatic approaches, we characterized the fold potential diversity of the amino acid sequences encoded by all intergenic open reading frames (ORFs) of S. cerevisiae with the aim of (1) exploring whether the structural states’ diversity of proteomes is already present in noncoding sequences, and (2) estimating the potential of the noncoding genome to produce novel protein bricks that could either give rise to novel genes or be integrated into pre-existing proteins, thus participating in protein structure diversity and evolution. We showed that amino acid sequences encoded by most yeast intergenic ORFs contain the elementary building blocks of protein structures. Moreover, they encompass the large structural state diversity of canonical proteins, with the majority predicted as foldable. Then, we investigated the early stages of de novo gene birth by reconstructing the ancestral sequences of 70 yeast de novo genes and characterized the sequence and structural properties of intergenic ORFs with a strong translation signal. This enabled us to highlight sequence and structural factors determining de novo gene emergence. Finally, we showed a strong correlation between the fold potential of de novo proteins and one of their ancestral amino acid sequences, reflecting the relationship between the noncoding genome and the protein structure universe.

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