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Your search keyword '"consensus sequences"' showing total 4 results
Start Over Descriptor "consensus sequences" Topic amino acids
4 results on '"consensus sequences"'

1. Endogenous Brevidensovirus-like elements in Cherax quadricarinatus: Friend or foe?

Author

Rusaini, La Fauce, Kathy A., Elliman, Jennifer, Bowater, Rachel O., and Owens, Leigh

Subjects
*CHERAX quadricarinatus, *FRESHWATER fishes, *CRAYFISH, *VIRUS-like particles, *FISH viruses
Abstract

Abstract: Nine endogenous Brevidensovirus-like elements (EBreVE) were identified in redclaw freshwater crayfish Cherax quadricarinatus from different sources suggesting that these elements are widespread in redclaw in northern Queensland, Australia. These endogenous virus-like elements shared nucleotide identities (70–100%) and amino acid similarities (34–100%) with infectious hypodermal and haematopoietic necrosis virus (IHHNV) scientifically classified as Penaeus stylirostris densovirus (PstDNV). They may not have originated from IHHNV genomes, but could be derived from another uncharacterised member of the genus Brevidensovirus that share nucleotide similarities with IHHNV. The most striking feature of EBreVEs was that in each case, the segment (portion) of viral sequences inserted into the host genomes was from the same region of the viral genome and most likely derived from non-structural protein regions of ancestral virus, but they cannot be assembled into one consensus sequence. The EBreVEs may be inserted into the redclaw genomes following chronic or persistent infection by a corresponding virus that may have occurred as multiple independent integration events years ago leading to the accumulation of several integrated elements in their genomes. Histological examination and polymerase chain reaction (PCR) suggested that these insertions may have a protective function to their host. [Copyright &y& Elsevier]

Published
2013
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2. Nucleic Acid Binding of the RTN1-C C-Terminal Region: Toward the Functional Role of a Reticulon Protein

Author

Sonia Melino, Stefania Di Marco, Alessia Bellomaria, Ridvan Nepravishta, and Maurizio Paci

Subjects
Secondary, protein synthesis, Amino acid sequences, Peptide, Biochemistry, Consensus sequences, Membrane proteins, genetics, Amines, C-terminal regions, Peptide sequence, chemistry.chemical_classification, zinc, Bacterial, RTN1 protein, Binding properties, Biological functions, Deacetylation, Histone deacetylase, Histone proteins, In-vivo, N terminals, Nervous systems, Spectroscopic techniques, Vesicle trafficking, Acetylation, Amino acids, Binding energy, Nucleic acids, Organic acids, Proteins, Zinc, Biomolecules, histone deacetylase 8, histone H4, membrane protein, nucleic acid, protein RTN1 C, reticulon, unclassified drug, bacterial DNA, bacterial RNA, DNA, nerve protein, protein, RNA, RTN1 protein, human, acetylation, amino acid sequence, article, carboxy terminal sequence, deacetylation, electrophoresis, endoplasmic reticulum, fluorescence, in vivo study, kinetics, membrane vesicle, molecular interaction, priority journal, protein conformation, protein localization, protein protein interaction, regulatory mechanism, sequence homology, binding site, biophysics, chemistry, consensus sequence, Escherichia coli, human, isolation and purification, metabolism, molecular genetics, protein binding, protein motif, protein processing, protein secondary structure, Amino Acid Motifs, Amino Acid Sequence, Binding Sites, Biophysical Processes, Consensus Sequence, DNA, Bacterial, Humans, Molecular Sequence Data, Nerve Tissue Proteins, Protein Binding, Protein Conformation, Protein Processing, Post-Translational, Protein Structure, Secondary, RNA, Bacterial, Histone, Protein Structure, Biophysical Phenomena, Consensus sequence, Settore BIO/10, Post-Translational, Reticulon, biology, Nucleic acid structure, Membrane protein, biology.protein, Nucleic acid
Abstract

RTN1-C protein is a membrane protein localized in the ER and expressed in the nervous system. Its biological role is still unclear, although interactions of the N-terminal region of RTN1-C with proteins involved in vesicle trafficking have been observed, but the role of the C-terminal region of this family protein remains to be investigated. By a homology analysis of the amino acid sequence, we identified in the C-terminal region of RTN1-C a unique consensus sequence characteristic of H4 histone protein. Thus, a 23-mer peptide (RTN1-C(CT)) corresponding to residues 186-208 of RTN1-C was synthesized, and its conformation and its interaction with nucleic acids were investigated. Here we demonstrate the strong ability of RTN1-C(CT) peptide to bind and condense the nucleic acids using electrophoretic and spectroscopic techniques. To determine if the binding of RTN1-C to nucleic acids could be regulated in vivo by an acetylation-deacetylation mechanism, as for the histone proteins, we studied the interaction of RTN1-C with one zinc-dependent histone deacetylase (HDAC) enzyme, HDAC8, with fluorescence and kinetic techniques using an acetylated form of RTN1-C(CT). The results reported here allow us to propose that the nucleic acid binding property of RTN1-C may have an important role in the biological function of this protein, the function of which could be regulated by an acetylation-deacetylation mechanism.

Published
2008
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