Reversible thermal unfolding of Bacillus subtilis levansucrase is modulated by Fe3+ and Ca2+
Open Access
- 26 November 1990
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 275 (1-2) , 61-64
- https://doi.org/10.1016/0014-5793(90)81439-u
Abstract
The equilibrium transition curves for thermal unfolding of levansucrase were established at several pH values. At pH 7 and within the temperature range of bacterial growth, the unfolded from is predominant. However, under such conditions, refolding is promoted by the only addition of Ca2+ or Fe3+. We propose that the tertiary structure flexibility of levansucrase plays a key role in its secretion process.Keywords
This publication has 11 references indexed in Scilit:
- Secretory S complex of Bacillus subtilis: sequence analysis and identity to pyruvate dehydrogenaseJournal of Bacteriology, 1990
- Secretion of Bacillus subtilis levansucrase. Fe(III) could act as a cofactor in an efficient coupling of the folding and translocation processesBiochemical Journal, 1990
- Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.The EMBO Journal, 1989
- Preprotein conformation: the year's major theme in translocation studiesTrends in Biochemical Sciences, 1988
- The ‘molten globule’ state is involved in the translocation of proteins across membranes?FEBS Letters, 1988
- Secretion of Bacillus subtilis levansucrase: a possible two‐step mechanismEuropean Journal of Biochemistry, 1987
- The structure of BAcillus subtilis levansucrase at 3.8 A resolution.Journal of Biological Chemistry, 1980
- Proton chemical potential, proton electrical potential and bacterial motilityJournal of Molecular Biology, 1980
- Occurrence and function of membrane teichoic acidsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1977
- [86] Levansucrase from Bacillus subtilisPublished by Elsevier ,1966