期刊
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
卷 1790, 期 10, 页码 1274-1281出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagen.2009.06.008
关键词
Scramblase; Peptides; Phospholipids; Calcium binding; Tryptophan fluorescence; Isothermal titration calorimetry
资金
- Center for Scientific and Industrial Research, New Delhi
Background: Phospholipid scramblases are a group of four homologous proteins conserved from C elegans to human. In human, two members of the scramblase family, hPLSCR1 and hPLSCR3 are known to bring about Ca2+ dependent translocation of phosphatidylserine and cardiolipin respectively during apoptotic processes. However, affinities of Ca2+/Mg2+ binding to human scramblases and conformational changes taking place in them remains unknown. Methods: In the present study, we analyzed the Ca2+ and Mg2+ binding to the calcium binding motifs of hPLSCR1-4 and hPLSCR1 by spectroscopic methods and isothermal titration calorimetry. Results: The results in this study show that (i) affinities of the peptides are in the order hPLSCR1 > hPLSCR3 > hPLSCR2 > hPLSCR4 for Ca2+ and in the order hPLSCR1 > hPLSCR2 > hPLSCR3 > hPLSCR4 for Mg2+, (ii) binding of ions brings about conformational change in the secondary structure of the peptides. The affinity of Ca2+ and Mg2+ binding to protein hPLSCR1 was similar to that of the peptide I. A sequence comparison shows the existence of scramblase-like motifs among other protein families. Conclusions: Based on the above results, we hypothesize that the Ca2+ binding motif of hPLSCR1 is a novel type of Ca2+ binding motif. General significance: Our findings will be relevant in understanding the calcium dependent scrambling activity of hPLSCRs and their biological function. (C) 2009 Elsevier B.V. All rights reserved.
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