Biological Activity and the 3-methylhistidine Content of Actin and Myosin

Overview

Journal Biochem J

Specialty Biochemistry

Date 1970 Sep 1

PMID 4249861

Citations 16

Authors

P Johnson

S V PERRY

Affiliations

Soon will be listed here.

Abstract

1. The 3-methylhistidine content of myosin varies according to muscle type. It is highest in myosin from white skeletal muscle and lower values are obtained from myosin of red skeletal and smooth muscle. 2. The 3-methylhistidine content of actin was similar in all of the types of muscle from which it was isolated. 3. The 3-methylhistidine of rabbit actin is localized in a single tryptic peptide that was readily modified during fractionation procedures. 4. Photo-oxidation studies indicated that the 3-methylhistidine residues are not essential for adeonsine triphosphatase and actin-combining activities of myosin. 5. During photooxidation G-actin lost completely the ability to polymerize to the F form before all the 3-methylhistidine was destroyed.

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References

Trayer I, Harris C, PERRY S . 3-Methyl histidine and adult and foetal forms of skeletal muscle myosin. Nature. 1968; 217(5127):452-3. DOI: 10.1038/217452a0. View

Johnson P, PERRY S . Chemical studies on the cysteine and terminal peptides in tryptic digests of actin. Biochem J. 1968; 110(2):207-16. PMC: 1187199. DOI: 10.1042/bj1100207. View

Stracher A . EVIDENCE FOR HISTIDINE AT THE ACTIVE SITE OF MYOSIN A. J Biol Chem. 1965; 240:958-60. View

Asatoor A, Armstrong M . 3-methylhistidine, a component of actin. Biochem Biophys Res Commun. 1967; 26(2):168-74. DOI: 10.1016/0006-291x(67)90229-x. View

Barany M, Nagy B, FINKELMAN F, Chrambach A . Studies on the removal of the bound nucleotide of actin. J Biol Chem. 1961; 236:2917-25. View

Johnson P, Harris C, PERRY S . 3-methylhistidine in actin and other muscle proteins. Biochem J. 1967; 105(1):361-70. PMC: 1198308. DOI: 10.1042/bj1050361. View

DE VILLAFRANCA G . Some physico-chemical properties of myosin B from the horseshoe crab, Limulus polyphemus. Comp Biochem Physiol. 1968; 26(2):443-54. DOI: 10.1016/0010-406x(68)90637-3. View

KIELLEY W, BRADLEY L . The relationship between sulfhydryl groups and the activation of myosin adenosinetriphosphatase. J Biol Chem. 1956; 218(2):653-9. View

Needham D, Williams J . PROTEINS OF THE UTERINE CONTRACTILE MECHANISM. Biochem J. 1963; 89:552-61. PMC: 1202462. DOI: 10.1042/bj0890552. View

10.

Hardy M, PERRY S . In vitro methylation of muscle proteins. Nature. 1969; 223(5203):300-2. DOI: 10.1038/223300a0. View

11.

Gershman L, Dreizen P, Stracher A . Subunit structure of myosin, II. Heavy and light alkali components. Proc Natl Acad Sci U S A. 1966; 56(3):966-73. PMC: 219954. DOI: 10.1073/pnas.56.3.966. View

12.

Martonosi A, GOUVEA M . Studies on actin. V. Chemical modification of actin. J Biol Chem. 1961; 236:1338-44. View

13.

Bailey K . Myosin and adenosinetriphosphatase. Biochem J. 1942; 36(1-2):121-39. PMC: 1265670. DOI: 10.1042/bj0360121. View

14.

Martonosi A . The sulfhydryl groups of actin. Arch Biochem Biophys. 1968; 123(1):29-40. DOI: 10.1016/0003-9861(68)90100-8. View

15.

WOODS E, HIMMELFARB S, Harrington W . Studies on the structure of myosin in solution. J Biol Chem. 1963; 238:2374-85. View

16.

PERRY S, Cotterill J . Interaction of actin and myosin. Nature. 1965; 206(980):161-3. DOI: 10.1038/206161a0. View

17.

NOLTMANN E, MAHOWALD T, KUBY S . Studies on adenosine triphosphate transphosphorylases. II. Amino acid composition of adenosine triphosphate-creatine transphosphorylase. J Biol Chem. 1962; 237:1146-54. View

18.

Hotta K . A model for the myosin ATPase active site. J Biochem. 1961; 50:218-29. DOI: 10.1093/oxfordjournals.jbchem.a127437. View