Linked Life Data

19140693

Source:http://linkedlifedata.com/resource/pubmed/id/19140693

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-1-14
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1520-4995
pubmed:author
pubmed:issnType
Electronic
pubmed:day
20
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
242-53
pubmed:meshHeading
pubmed-meshheading:19140693-Amino Acid Motifs, pubmed-meshheading:19140693-Amino Acid Sequence, pubmed-meshheading:19140693-Binding Sites, pubmed-meshheading:19140693-Biophysical Processes, pubmed-meshheading:19140693-Consensus Sequence, pubmed-meshheading:19140693-DNA, pubmed-meshheading:19140693-DNA, Bacterial, pubmed-meshheading:19140693-Escherichia coli, pubmed-meshheading:19140693-Humans, pubmed-meshheading:19140693-Molecular Sequence Data, pubmed-meshheading:19140693-Nerve Tissue Proteins, pubmed-meshheading:19140693-Protein Binding, pubmed-meshheading:19140693-Protein Conformation, pubmed-meshheading:19140693-Protein Processing, Post-Translational, pubmed-meshheading:19140693-Protein Structure, Secondary, pubmed-meshheading:19140693-Proteins, pubmed-meshheading:19140693-RNA, pubmed-meshheading:19140693-RNA, Bacterial
pubmed:year
2009
pubmed:articleTitle
Nucleic acid binding of the RTN1-C C-terminal region: toward the functional role of a reticulon protein.
pubmed:affiliation
Department of Sciences and Chemical Technologies, University of Rome Tor Vergata, Rome, Italy. melinos@uniroma2.it
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't