Linked Life Data

9671503

Source:http://linkedlifedata.com/resource/pubmed/id/9671503

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
1998-8-5
pubmed:abstractText
Assembly of the three neuronal membrane proteins synaptobrevin, syntaxin, and SNAP-25 is thought to be one of the key steps in mediating exocytosis of synaptic vesicles. In vivo and in vitro, these proteins form a tight complex. Assembly is associated with a large increase in alpha-helical content, suggesting that major structural and conformational changes are associated with the assembly reaction. Limited proteolysis by trypsin, chymotrypsin, and proteinase K of the ternary complex formed from recombinant proteins lacking their membrane anchors revealed a SDS-resistant minimal core. The components of this core complex were purified and characterized by N-terminal sequencing and mass spectrometry. They include a slightly shortened synaptobrevin fragment, C- and N-terminal fragments of SNAP-25, and a C-terminal fragment of syntaxin that is slightly larger than the previously characterized H3 domain. Recombinant proteins corresponding to these fragments are sufficient for assembly and disassembly. In addition, each of the two SNAP-25 fragments can individually form complexes with syntaxin and synaptobrevin, suggesting that they both contribute to the assembly of the SNARE complex. Upon complex assembly, a large increase in alpha-helical content is observed along with a significantly increased melting temperature (Tm). Like the full-length complex, the minimal complex tends to form an oligomeric species; global analysis of equilibrium ultracentrifugation data suggests a monomer-trimer equilibrium exists. These conserved biophysical properties may thus be of fundamental importance in the mechanism of membrane fusion.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10354-62
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9671503-Amino Acid Sequence, pubmed-meshheading:9671503-Animals, pubmed-meshheading:9671503-Circular Dichroism, pubmed-meshheading:9671503-Endopeptidases, pubmed-meshheading:9671503-Hydrolysis, pubmed-meshheading:9671503-Macromolecular Substances, pubmed-meshheading:9671503-Membrane Proteins, pubmed-meshheading:9671503-Molecular Sequence Data, pubmed-meshheading:9671503-Nerve Tissue Proteins, pubmed-meshheading:9671503-Qa-SNARE Proteins, pubmed-meshheading:9671503-R-SNARE Proteins, pubmed-meshheading:9671503-Rats, pubmed-meshheading:9671503-SNARE Proteins, pubmed-meshheading:9671503-Structure-Activity Relationship, pubmed-meshheading:9671503-Synaptic Vesicles, pubmed-meshheading:9671503-Synaptosomal-Associated Protein 25, pubmed-meshheading:9671503-Vesicular Transport Proteins
pubmed:year
1998
pubmed:articleTitle
Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly.
pubmed:affiliation
Department of Neurobiology, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't