The primary structure and analysis of the squid kinesin heavy chain

Kenneth S. Kosik, Lisa D. Orecchio, Bruce Schnapp, Hideyo Inouye, Rachael L. Neve

Research output: Contribution to journalArticle

76 Citations (Scopus)

Abstract

We report the cDNA sequence of the squid kinesin heavy chain and compared the predicted amino acid sequence with that of the Drosophila heavy chain as reported by Yang, J. T., Lay mon, R. A., and Goldstein, L. S. B. (1989) Cell 56, 879-889). We compared the two kinesin sequences with regard to the predicted physicochemical parameters of hydrophobicity, charge, and propensities of the secondary conformations. A comparison of the sequences from the two species reveals the head, stalk, and tail domains because a reduced degree of conservation demarcates the stalk. The charge profile indicates that the head region is nearly neutral, the stalk region acidic, and the tail is basic. The Fourier transform analysis of the hydrophobic profile of the stalk shows predominant peaks at 1/3.5 and 1/2.3, which are indexed as the second and third orders of the period 7 residue. As in the Drosophila sequence, the rod domain is divided into an amino and a carboxyl subdomain by a predicted hinge region. We show that the disposition of hydrophobic residues is distinct in these two subdomains. In particular, the heptad repeat is more regular in the aminoterminal rod domain than in the carboxyl-terminal rod domain. The tail region is positively charged, a feature that is consistent with the known electrostatic interaction between the heavy chain and negatively charged surfaces such as glass coverslips and latex beads. Three monoclonal antibodies to the kinesin heavy chain have been mapped to a region within the carboxyl terminus of the stalk.

Original languageEnglish (US)
Pages (from-to)3278-3283
Number of pages6
JournalJournal of Biological Chemistry
Volume265
Issue number6
StatePublished - Feb 25 1990
Externally publishedYes

Fingerprint

Kinesin
Decapodiformes
Tail
Fourier Analysis
Drosophila
Latex
Hinges
Hydrophobicity
Coulomb interactions
Static Electricity
Microspheres
Hydrophobic and Hydrophilic Interactions
Glass
Conformations
Amino Acid Sequence
Conservation
Fourier transforms
Complementary DNA
Head
Monoclonal Antibodies

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kosik, K. S., Orecchio, L. D., Schnapp, B., Inouye, H., & Neve, R. L. (1990). The primary structure and analysis of the squid kinesin heavy chain. Journal of Biological Chemistry, 265(6), 3278-3283.

The primary structure and analysis of the squid kinesin heavy chain. / Kosik, Kenneth S.; Orecchio, Lisa D.; Schnapp, Bruce; Inouye, Hideyo; Neve, Rachael L.

In: Journal of Biological Chemistry, Vol. 265, No. 6, 25.02.1990, p. 3278-3283.

Research output: Contribution to journalArticle

Kosik, KS, Orecchio, LD, Schnapp, B, Inouye, H & Neve, RL 1990, 'The primary structure and analysis of the squid kinesin heavy chain', Journal of Biological Chemistry, vol. 265, no. 6, pp. 3278-3283.
Kosik KS, Orecchio LD, Schnapp B, Inouye H, Neve RL. The primary structure and analysis of the squid kinesin heavy chain. Journal of Biological Chemistry. 1990 Feb 25;265(6):3278-3283.
Kosik, Kenneth S. ; Orecchio, Lisa D. ; Schnapp, Bruce ; Inouye, Hideyo ; Neve, Rachael L. / The primary structure and analysis of the squid kinesin heavy chain. In: Journal of Biological Chemistry. 1990 ; Vol. 265, No. 6. pp. 3278-3283.
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