Characterization of calretinin I-II as an EF-hand, Ca2+, H+-sensing domain
(2005) In Protein Science 14(7). p.1879-1887- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/151508
- author
- Palczewska, M ; Batta, G ; Groves, P ; Linse, Sara LU and Kuznicki, J
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Protein Science
- volume
- 14
- issue
- 7
- pages
- 1879 - 1887
- publisher
- The Protein Society
- external identifiers
-
- wos:000230253900019
- pmid:15937279
- scopus:22244462446
- pmid:15937279
- ISSN
- 1469-896X
- DOI
- 10.1110/ps.051369805
- language
- English
- LU publication?
- yes
- id
- 39953043-03a7-4c47-8639-30f34f3fc992 (old id 151508)
- date added to LUP
- 2016-04-01 12:10:27
- date last changed
- 2022-03-05 20:00:25
@article{39953043-03a7-4c47-8639-30f34f3fc992,
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.}},
author = {{Palczewska, M and Batta, G and Groves, P and Linse, Sara and Kuznicki, J}},
issn = {{1469-896X}},
language = {{eng}},
number = {{7}},
pages = {{1879--1887}},
publisher = {{The Protein Society}},
series = {{Protein Science}},
title = {{Characterization of calretinin I-II as an EF-hand, Ca2+, H+-sensing domain}},
url = {{http://dx.doi.org/10.1110/ps.051369805}},
doi = {{10.1110/ps.051369805}},
volume = {{14}},
year = {{2005}},
}