Ca2+-induced structural change in the Ca2+ Mg2+ domain of troponin C detected by crosslinking

Valentina V. Kareva, Anatoly B. Dobrovol'sky, Ludmila A. Baratova, P. Friedrich, Nikolai B. Gusev

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Abstract

Rabbit muscle troponin C was selectively modified at Cys-98 by 1,3-difluoro-4,6-dinitrobenzene. The second function of the bifunctional reagent was triggered at alkaline pH in the presence and absence of Ca2+. The crosslinked troponin C was hydrolyzed by trypsin and the peptides containing a dinitrobenzene moiety were isolated. When troponin C was crosslinked in the presence of Ca2+, the single dinitrobenzene-containing peptide was Gly-89-Arg-100, in which Cys-98 was crosslinked with Lys-90. When crosslinking was performed in the absence of Ca2+, beside the above peptide two additional peptides containing dinitrobenzene were found. One of these peptides is made up of two fragments, Ser-91-Arg-100 and Asn-105-Arg-120, crosslinked between Cys-98 and Tyr-109. The second peptide, Ala-121-Lys-140, contains modified Lys-136, presumably crosslinked with His-135. The data indicate that the distances between the α-carbon of Cys-98 and those of Lys-90, Tyr-109, Lys-136 and probably the α-carbon distance His-125-Lys-136, do not exceed 14 Å. Comparison with the X-ray structure of troponin C (Herzberg, O, and James, M.N.G. (1985) Nature 313, 653-659) indicates that some of the above distances increase on Ca2+-binding.

Original languageEnglish
Pages (from-to)322-329
Number of pages8
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume869
Issue number3
DOIs
Publication statusPublished - Feb 14 1986

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Troponin C
Crosslinking
Dinitrobenzenes
Peptides
Carbon
Cross-Linking Reagents
Trypsin
Muscle
X-Rays
Rabbits
X rays
Muscles

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology
  • Medicine(all)

Cite this

Ca2+-induced structural change in the Ca2+ Mg2+ domain of troponin C detected by crosslinking. / Kareva, Valentina V.; Dobrovol'sky, Anatoly B.; Baratova, Ludmila A.; Friedrich, P.; Gusev, Nikolai B.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 869, No. 3, 14.02.1986, p. 322-329.

Research output: Contribution to journalArticle

Kareva, Valentina V. ; Dobrovol'sky, Anatoly B. ; Baratova, Ludmila A. ; Friedrich, P. ; Gusev, Nikolai B. / Ca2+-induced structural change in the Ca2+ Mg2+ domain of troponin C detected by crosslinking. In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular. 1986 ; Vol. 869, No. 3. pp. 322-329.
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abstract = "Rabbit muscle troponin C was selectively modified at Cys-98 by 1,3-difluoro-4,6-dinitrobenzene. The second function of the bifunctional reagent was triggered at alkaline pH in the presence and absence of Ca2+. The crosslinked troponin C was hydrolyzed by trypsin and the peptides containing a dinitrobenzene moiety were isolated. When troponin C was crosslinked in the presence of Ca2+, the single dinitrobenzene-containing peptide was Gly-89-Arg-100, in which Cys-98 was crosslinked with Lys-90. When crosslinking was performed in the absence of Ca2+, beside the above peptide two additional peptides containing dinitrobenzene were found. One of these peptides is made up of two fragments, Ser-91-Arg-100 and Asn-105-Arg-120, crosslinked between Cys-98 and Tyr-109. The second peptide, Ala-121-Lys-140, contains modified Lys-136, presumably crosslinked with His-135. The data indicate that the distances between the α-carbon of Cys-98 and those of Lys-90, Tyr-109, Lys-136 and probably the α-carbon distance His-125-Lys-136, do not exceed 14 {\AA}. Comparison with the X-ray structure of troponin C (Herzberg, O, and James, M.N.G. (1985) Nature 313, 653-659) indicates that some of the above distances increase on Ca2+-binding.",
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