Characterization of calretinin I-II as an EF-hand, Ca2+, H +-sensing domain

Małgorzata Palczewska, G. Batta, Patrick Groves, Sara Linse, Jacek Kuźnicki

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Calretinin, a neuronal protein with well-defined calcium-binding properties, has a poorly defined function. The pH dependent properties of calretinin (CR), the N-terminal (CR I-II), and C-terminal (CR III-VI) domains were investigated. A drop in pH within the intracellular range (from pH 7.5 to pH 6.5) leads to an increased hydrophobicity of calcium-bound CR and its domains as reported by fluorescence spectroscopy with the hydrophobic probe 2-(p-toluidino)-6-naphthalenesulfonic acid (TNS). The TNS data for the N- and C-terminal domains of CR are additive, providing further support for their independence within the full-length protein. Our work concentrated on CR I-II, which was found to have hydrophobic properties similar to calmodulin at lower pH. The elution of CR I-II from a phenyl-Sepharose column was consistent with the TNS data. The pH-dependent structural changes were further localized to residues 13-28 and 44-51 using nuclear magnetic resonance spectroscopy chemical shift analysis, and there appear to be no large changes in secondary structure. Protonation of His12 and/or His27 side chains, coupled with calcium chelation, appears to lead to the organization of a hydrophobic pocket in the N-terminal domain. CR may sense and respond to calcium, proton, and other signals, contributing to conflicting data on the proteins role as a calcium sensor or calcium buffer.

Original languageEnglish
Pages (from-to)1879-1887
Number of pages9
JournalProtein Science
Volume14
Issue number7
DOIs
Publication statusPublished - Jul 2005

Fingerprint

EF Hand Motifs
Calbindin 2
Calcium
Proteins
Protonation
Fluorescence Spectrometry
Fluorescence spectroscopy
Chemical shift
Calmodulin
Hydrophobicity
Chelation
Hydrophobic and Hydrophilic Interactions
Nuclear magnetic resonance spectroscopy
Protons
Buffers
Magnetic Resonance Spectroscopy

Keywords

  • Calbindin D28k
  • Calcium
  • Calretinin
  • EF-hand
  • Ischemia
  • pH response

ASJC Scopus subject areas

  • Biochemistry

Cite this

Characterization of calretinin I-II as an EF-hand, Ca2+, H +-sensing domain. / Palczewska, Małgorzata; Batta, G.; Groves, Patrick; Linse, Sara; Kuźnicki, Jacek.

In: Protein Science, Vol. 14, No. 7, 07.2005, p. 1879-1887.

Research output: Contribution to journalArticle

Palczewska, M, Batta, G, Groves, P, Linse, S & Kuźnicki, J 2005, 'Characterization of calretinin I-II as an EF-hand, Ca2+, H +-sensing domain', Protein Science, vol. 14, no. 7, pp. 1879-1887. https://doi.org/10.1110/ps.051369805
Palczewska, Małgorzata ; Batta, G. ; Groves, Patrick ; Linse, Sara ; Kuźnicki, Jacek. / Characterization of calretinin I-II as an EF-hand, Ca2+, H +-sensing domain. In: Protein Science. 2005 ; Vol. 14, No. 7. pp. 1879-1887.
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