Phosphorylation of the sarcoplasmic reticulum Ca(2+)-ATPase from ATP and ATP analogs studied by infrared spectroscopy

The Journal of Biological Chemistry
Man Liu, Andreas Barth

Abstract

Phosphorylation of the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a) was studied with time-resolved Fourier transform infrared spectroscopy. ATP and ATP analogs (ITP, 2'- and 3'-dATP) were used to study the effect of the adenine ring and the ribose hydroxyl groups on ATPase phosphorylation. All modifications of ATP altered conformational changes and phosphorylation kinetics. The differences compared with ATP increased in the following order: 3'-dATP > ITP > 2'-dATP. Enzyme phosphorylation with ITP results in larger absorbance changes in the amide I region, indicating larger conformational changes of the Ca(2+)-ATPase. The respective absorbance changes obtained with 3'-dATP are significantly different from the others with different band positions and amplitudes in the amide I region, indicating different conformational changes of the protein backbone. ATPase phosphorylation with 3'-dATP is also much ( approximately 30 times) slower than with ATP. Our results indicate that modifications to functional groups of ATP (the ribose 2'- and 3'-OH and the amino group in the adenine ring) affect gamma-phosphate transfer to the phosphorylation site of the Ca(2+)-ATPase by changing the extent of conformational change and the phosphorylatio...Continue Reading

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Citations

Sep 3, 2010·Quarterly Reviews of Biophysics·Jesper V MøllerPoul Nissen
May 3, 2008·Journal of Cellular Biochemistry·Brenda Schoffstall, P Bryant Chase
Dec 13, 2006·Biochimica Et Biophysica Acta·Maria Krasteva, Andreas Barth
Nov 16, 2013·The Journal of Physical Chemistry. B·Nadejda Eremina, Andreas Barth
Aug 19, 2007·Biochimica Et Biophysica Acta·Andreas Barth
Oct 2, 2007·Biochimica Et Biophysica Acta·Eeva-Liisa KarjalainenAndreas Barth

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