Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
1995-1-12
pubmed:abstractText
Tektins are proteins that copartition with tubulin in a stable ribbon of three protofilaments from ciliary and flagellar microtubules. After purification, tektins A, B, and C from sea urchin sperm flagellar microtubules appear as extended relatively insoluble filaments, < 5 nm in diameter. We used cross-linking reagents to investigate the associations and structural organization of subunits within tektin polymers isolated from stable protofilament ribbons of Strongylocentrotus purpuratus. We show by SDS-polyacrylamide gel electrophoresis, immunoblots, and transmission electron microscopy that tektins are continuous heteropolymers in the stable protofilament ribbons, and thus flagellar microtubules. Our results also provide evidence for the arrangement of different tektin polypeptides within "core" filaments containing equimolar tektins A and B. Treatment of these core filaments with bis(sulfosuccinimidyl)suberate and with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide yielded a predominant cross-linked approximately 106-kDa heterodimer of tektins A and B; similar results were obtained by glutaraldehyde cross-linking of tektins solubilized under mild conditions. Finally, cross-linking with 3,3'-dithiobis(sulfosuccinimidylpropionate) revealed a 16 nm periodicity in isolated tektin AB filaments that can be related to the 8 nm tubulin dimer lattice and to periodically associated microtubule components.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31800-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Tektins are heterodimeric polymers in flagellar microtubules with axial periodicities matching the tubulin lattice.
pubmed:affiliation
Department of Cell Biology and Neuroanatomy, University of Minnesota, Minneapolis 55455.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.