Study on the Chaperone Properties of Conserved GTPases

Overview

Journal Protein Cell

Publisher Oxford University Press

Specialties Biochemistry
Cell Biology

Date 2012 Jan 17

PMID 22246579

Authors

Xiang Wang

Jiaying Xue

Zhe Sun

Yan Qin

Weimin Gong

Affiliations

Soon will be listed here.

Abstract

As a large family of hydrolases, GTPases are widespread in cells and play the very important biological function of hydrolyzing GTP into GDP and inorganic phosphate through binding with it. GTPases are involved in cell cycle regulation, protein synthesis, and protein transportation. Chaperones can facilitate the folding or refolding of nascent peptides and denatured proteins to their native states. However, chaperones do not occur in the native structures in which they can perform their normal biological functions. In the current study, the chaperone activity of the conserved GTPases of Escherichia coli is tested by the chemical denaturation and chaperone-assisted renaturation of citrate synthase and α-glucosidase. The effects of ribosomes and nucleotides on the chaperone activity are also examined. Our data indicate that these conserved GTPases have chaperone properties, and may be ancestral protein folding factors that have appeared before dedicated chaperones.

References

Deuerling E, Tomoyasu T, Mogk A, Bukau B . Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature. 1999; 400(6745):693-6. DOI: 10.1038/23301. View

Leipe D, Wolf Y, Koonin E, Aravind L . Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol. 2002; 317(1):41-72. DOI: 10.1006/jmbi.2001.5378. View

Ellis R . The general concept of molecular chaperones. Philos Trans R Soc Lond B Biol Sci. 1993; 339(1289):257-61. DOI: 10.1098/rstb.1993.0023. View

Maier R, Scholz C, Schmid F . Dynamic association of trigger factor with protein substrates. J Mol Biol. 2001; 314(5):1181-90. DOI: 10.1006/jmbi.2000.5192. View

Jakob U, Gaestel M, Engel K, Buchner J . Small heat shock proteins are molecular chaperones. J Biol Chem. 1993; 268(3):1517-20. View

Ellis R . The molecular chaperone concept. Semin Cell Biol. 1990; 1(1):1-9. View

Caldas T, El Yaagoubi A, Richarme G . Chaperone properties of bacterial elongation factor EF-Tu. J Biol Chem. 1998; 273(19):11478-82. DOI: 10.1074/jbc.273.19.11478. View

Nissen P, Hansen J, Ban N, Moore P, Steitz T . The structural basis of ribosome activity in peptide bond synthesis. Science. 2000; 289(5481):920-30. DOI: 10.1126/science.289.5481.920. View

Ellis R, Hemmingsen S . Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem Sci. 1989; 14(8):339-42. DOI: 10.1016/0968-0004(89)90168-0. View

10.

Kramer G, Boehringer D, Ban N, Bukau B . The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nat Struct Mol Biol. 2009; 16(6):589-97. DOI: 10.1038/nsmb.1614. View

11.

Hartl F, Hayer-Hartl M . Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol. 2009; 16(6):574-81. DOI: 10.1038/nsmb.1591. View

12.

Caldas T, Laalami S, Richarme G . Chaperone properties of bacterial elongation factor EF-G and initiation factor IF2. J Biol Chem. 2000; 275(2):855-60. DOI: 10.1074/jbc.275.2.855. View

13.

Caldon C, Yoong P, March P . Evolution of a molecular switch: universal bacterial GTPases regulate ribosome function. Mol Microbiol. 2001; 41(2):289-97. DOI: 10.1046/j.1365-2958.2001.02536.x. View

14.

Marquez V, Wilson D, Tate W, Triana-Alonso F, Nierhaus K . Maintaining the ribosomal reading frame: the influence of the E site during translational regulation of release factor 2. Cell. 2004; 118(1):45-55. DOI: 10.1016/j.cell.2004.06.012. View

15.

Teter S, Houry W, Ang D, Tradler T, Rockabrand D, Fischer G . Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell. 1999; 97(6):755-65. DOI: 10.1016/s0092-8674(00)80787-4. View

16.

Hendrick J, Hartl F . Molecular chaperone functions of heat-shock proteins. Annu Rev Biochem. 1993; 62:349-84. DOI: 10.1146/annurev.bi.62.070193.002025. View

17.

Kudlicki W, Coffman A, Kramer G, Hardesty B . Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing. J Biol Chem. 1998; 272(51):32206-10. DOI: 10.1074/jbc.272.51.32206. View

18.

Genevaux P, Keppel F, Schwager F, Langendijk-Genevaux P, Hartl F, Georgopoulos C . In vivo analysis of the overlapping functions of DnaK and trigger factor. EMBO Rep. 2004; 5(2):195-200. PMC: 1298978. DOI: 10.1038/sj.embor.7400067. View

19.

Buskiewicz I, Deuerling E, Gu S, Jockel J, Rodnina M, Bukau B . Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor. Proc Natl Acad Sci U S A. 2004; 101(21):7902-6. PMC: 419529. DOI: 10.1073/pnas.0402231101. View

20.

Gu S, Peske F, Wieden H, Rodnina M, Wintermeyer W . The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome. RNA. 2003; 9(5):566-73. PMC: 1370422. DOI: 10.1261/rna.2196403. View