RNase A – tRNA binding alters protein conformation

C.N. N’soukpoé-Kossi; C. Ragi; H.A. Tajmir-Riahi

doi:10.1139/o07-050

journal article Jun 01, 2007

RNase A – tRNA binding alters protein conformation

C.N. N’soukpoé-Kossi C. Ragi H.A. Tajmir-Riahi

Biochemistry and Cell Biology Vol. 85 No. 3 pp. 311-318 · Canadian Science Publishing

View at Publisher Save 10.1139/o07-050

Abstract

Bovine pancreatic ribonuclease A (RNase A) catalyzes the cleavage of P-O5′ bonds in RNA on the 3′ side of pyrimidine to form cyclic 2′,5′-phosphates. Even though extensive structural information is available on RNase A complexes with mononucleotides and oligonucleotides, the interaction of RNase A with tRNA has not been fully investigated. We report the complexation of tRNA with RNase A in aqueous solution under physiological conditions, using a constant RNA concentration and various amounts of RNase A. Fourier transform infrared, UV-visible, and circular dichroism spectroscopic methods were used to determine the RNase binding mode, binding constant, sequence preference, and biopolymer secondary structural changes in the RNase–tRNA complexes. Spectroscopic results showed 2 major binding sites for RNase A on tRNA, with an overall binding constant of K = 4.0 × 105 (mol/L)–1. The 2 binding sites were located at the G-C base pairs and the backbone PO2 group. Protein–RNA interaction alters RNase secondary structure, with a major reduction in α helix and β sheets and an increase in the turn and random coil structures, while tRNA remains in the A conformation upon protein interaction. No tRNA digestion was observed upon RNase A complexation.

Topics

No keywords indexed for this article. Browse by subject →

References

46

[1]

FT-IR and Raman investigation of cadmium binding by DNA

Serge Alex, Paul Dupuis

Inorganica Chimica Acta 10.1016/s0020-1693(00)80552-6

[2]

10.1002/bip.10159

[3]

10.1261/rna.5163104

[4]

10.1107/s0907444901021758

[5]

10.1002/bip.360250307

[6]

10.1093/nar/28.7.1656

[7]

D’Alessio, G., and Riordan, J.F. 1997. Ribonucleases: structure and functions. Academic Press, New York.

[8]

10.1016/s0003-9861(03)00214-5

[9]

10.1002/bip.10165

[10]

10.1021/bi981369s

[11]

Fontecilla-Camps J.C. J. Biol. Chem. (1994) 10.1016/s0021-9258(17)31836-7

[12]

10.1146/annurev.biochem.67.1.153

[13]

10.1038/sj.cgt.7700742

[14]

10.1002/bip.10483

[15]

10.1074/jbc.m112227200

[16]

Johnson W.C. Funct. Genet. (1999)

[17]

10.1093/nar/29.4.943

[18]

10.1093/emboj/19.24.6908

[19]

10.1073/pnas.0506662102

[20]

Vibrational Spectroscopy and Conformation of Peptides, Polypeptides, and Proteins

Samuel Krimm, Jagdeesh Bandekar

Advances in Protein Chemistry 1986 10.1016/s0065-3233(08)60528-8

[21]

10.1002/bip.10112

[22]

10.1073/pnas.95.18.10407

[23]

10.1110/ps.03196603

[24]

DNA Interaction with Human Serum Albumin Studied by Affinity Capillary Electrophoresis and FTIR Spectroscopy

H. Malonga, J.F. Neault, H. Arakawa et al.

DNA and Cell Biology 10.1089/dna.2006.25.63

[25]

10.1089/dna.2006.25.393

[26]

10.1074/jbc.m302711200

[27]

Moras D. Curr. Opin. Struct. Biol. (1998) 10.1016/0959-440x(92)90189-e

[28]

10.1006/jmbi.1998.2365

[29]

10.1038/86228

[30]

Structural Analysis of DNA Interactions with Biogenic Polyamines and Cobalt(III)hexamine Studied by Fourier Transform Infrared and Capillary Electrophoresis

Amin Ahmed Ouameur, Heidar-Ali Tajmir-Riahi

Journal of Biological Chemistry 10.1074/jbc.m406053200

[31]

10.1529/biophysj.105.064667

[32]

Raines R.T. Chem. Rev. (1999) 10.1021/cr960427h

[33]

10.1021/ja01640a067

[34]

Thermally Denatured Ribonuclease A Retains Secondary Structure As Shown by FTIR

Sangita Seshadri, Keith A. Oberg, Anthony L. Fink

Biochemistry 10.1021/bi00172a010

[35]

Sharin E. Nucleic Acids Res. (2004) 10.1093/nar/gki828

[36]

The crystal structure of yeast phenylalanine tRNA at 1.93 Å resolution: A classic structure revisited

HUIJING SHI, Peter B. Moore

RNA 10.1017/s1355838200000364

[37]

Soucek J. Comp. Biochem. Physiol. (1999)

[38]

Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set

Narasimha Sreerama, Robert W. Woody

Analytical Biochemistry 10.1006/abio.2000.4880

[39]

Drug-protein interactions: Two-site binding of heterocyclic ligands to a monomeric hemoglobin

J Stephanos

Journal of Inorganic Biochemistry 10.1016/0162-0134(95)00144-1

[40]

Taillandier E. Methods Enzymol. (1992) 10.1016/0076-6879(92)11018-e

[41]

10.1146/annurev.biophys.27.1.407

[42]

10.1006/bbrc.2000.2707

[43]

Vorlickova M. Biophys. J. (1995) 10.1016/s0006-3495(95)80073-1

[44]

Vorlickova M. Biopolymers (1990) 10.1002/bip.360290210

[45]

10.1016/0022-2860(91)87138-8

[46]

The interaction of human serum albumin with a novel antidiabetic agent—SU-118

Wenying Zhong, Yuchun Wang, Jun-Sheng Yu et al.

Journal of Pharmaceutical Sciences 10.1002/jps.20005

Metrics

3

Citations

46

References

Details

Published: Jun 01, 2007
Vol/Issue: 85(3)
Pages: 311-318
License: View

Authors

C

C.N. N’soukpoé-Kossi

Department of Chemistry-Biology, Université du Québec at Trois-Rivières, C.P. 500 Trois-Rivières, QC G9A 5H7, Canada.

C

C. Ragi

Department of Chemistry-Biology, Université du Québec at Trois-Rivières, C.P. 500 Trois-Rivières, QC G9A 5H7, Canada.

H

H.A. Tajmir-Riahi

Department of Chemistry-Biology, Université du Québec at Trois-Rivières, C.P. 500 Trois-Rivières, QC G9A 5H7, Canada.

Cite This Article

C.N. N’soukpoé-Kossi, C. Ragi, H.A. Tajmir-Riahi (2007). RNase A – tRNA binding alters protein conformation. Biochemistry and Cell Biology, 85(3), 311-318. https://doi.org/10.1139/o07-050

RNase A – tRNA binding alters protein conformation

You May Also Like