title: Role of neck region in the thermal aggregation of myosin.
abstract: Carp dorsal myosin formed oligomers that retained ATPase activity upon heating. Cleavage of the oligomeric myosin at subfragment-1 (S-1)/rod junction released monomeric S-1 and rod, indicating that ATPase retaining myosin associated near the S-1/rod junction. The digest also contained rod oligomers. Heating a mixture of S-1 and rod generated neither ATPase retaining S-1 oligomers nor rod oligomers. Electron microscopic observation of the heated myosin revealed that some oligomers were formed by associating at the S-1/rod joining region, exhibiting a recognized double head, probably ATPase retaining oligomers. No myosin oligomers associated at the tail region were observed, thus, rod aggregation would be formed at its very restricted region near the S-1/rod junction. Based on the findings, we proposed that the neck structure is important in the thermal oligomerization process of myosin.
authors.affiliation: Laboratory of Marine Food Sciences, Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido 041-8611 Japan.
authors.forename: Tomoko
authors.initials: T
authors.lastname: Tazawa
authors.forename: Sanae
authors.initials: S
authors.lastname: Kato
authors.forename: Tsuyoshi
authors.initials: T
authors.lastname: Katoh
authors.forename: Kunihiko
authors.initials: K
authors.lastname: Konno
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D002347:Carps; D006358:Hot Temperature; D008854:Microscopy, Electron; D009218:Myosins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D011487:Protein Conformation; D011489:Protein Denaturation
chemical_list: D000251:Adenosine Triphosphatases; D009218:Myosins