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Different assembly properties of cod, bovine, and rat brain microtubules.

Artikel i vetenskaplig tidskrift
Författare B Fridén
E Strömberg
Margareta Wallin
Publicerad i Cell motility and the cytoskeleton
Volym 21
Nummer/häfte 4
Sidor 305-12
ISSN 0886-1544
Publiceringsår 1992
Publicerad vid Zoologiska institutionen
Sidor 305-12
Språk en
Länkar dx.doi.org/10.1002/cm.970210406
Ämnesord Animals, Brain Chemistry, Cattle, Electrophoresis, Polyacrylamide Gel, Estramustine, pharmacology, Fishes, Heparin, pharmacology, Macromolecular Substances, Microtubule-Associated Proteins, antagonists & inhibitors, chemistry, Microtubules, chemistry, drug effects, ultrastructure, Rats, Sodium Chloride, pharmacology
Ämneskategorier Biologiska vetenskaper, Cell- och molekylärbiologi

Sammanfattning

Assembly properties of cod, bovine, and rat brain microtubules were compared. Estramustine phosphate, heparin, poly-L-aspartic acid, as well as NaCl, inhibited the assembly and disassembled both bovine and rat microtubules by inhibition of the binding between tubulin and MAPs. The assembly of cod brain microtubules was in contrast only marginally affected by these agents, in spite of a release of the MAPs. The results suggest that cod tubulin has a high intrinsic ability to assemble. This was confirmed by studies on phosphocellulose-purified cod tubulin, since the critical concentration for assembly was independent of the presence or absence of MAPs. The results show therefore that cod brain tubulin has, in contrast to bovine and rat brain tubulins, a high propensity to assembly under conditions which normally require the presence of MAPs. Even if cod MAPs, which have an unusual protein composition, were not needed for the assembly of cod microtubules, they were able to induce assembly of bovine brain tubulin. Both cod and bovine MAPs bound to cod microtubules, and bovine MAP1 and MAP2 bound to, and substituted at least the 400 kDa cod protein. This suggests that the tubulin-binding sites and the assembly-stimulatory ability of MAPs are common properties of MAPs from different species, independent of the tubulin assembly propensity.

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