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The exclusion of glycine betaine from anionic biopolymer surface: why glycine betaine is an effective osmoprotectant but also a compatible solute.
Biochemistry. 2004 Nov 23; 43(46):14732-43.B

Abstract

Paradoxically, glycine betaine (N,N,N-trimethyl glycine; GB) in vivo is both an effective osmoprotectant (efficient at increasing cytoplasmic osmolality and growth rate) and a compatible solute (without deleterious effects on biopolymer function, including stability and activity). For GB to be an effective osmoprotectant but not greatly affect biopolymer stability, we predict that it must interact very differently with folded protein surface than with that exposed in unfolding. To test this hypothesis, we quantify the preferential interaction of GB with the relatively uncharged surface exposed in unfolding the marginally stable lacI helix-turn-helix (HTH) DNA binding domain using circular dichroism and with the more highly charged surfaces of folded hen egg white lysozyme (HEWL) and bovine serum albumin (BSA) using all-gravimetric vapor pressure osmometry (VPO) and compare these results with results of VPO studies (Hong et al. (2004), Biochemistry, 43, 14744-14758) of the interaction of GB with polyanionic duplex DNA. For these four biopolymer surfaces, we observe that the extent of exclusion of GB per unit of biopolymer surface area increases strongly with increasing fraction of anionic oxygen (protein carboxylate or DNA phosphate) surface. In addition, GB is somewhat more excluded from the surface exposed in unfolding the lacI HTH and from the folded surface of HEWL than expected from their small fraction of anionic surface, consistent with moderate exclusion of GB from polar amide surface, as predicted by the osmophobic model of protein stability (Bolen and Baskakov (2001) J. Mol. Biol. 310, 955-963). Strong exclusion of GB from anionic surface explains how it can be both an effective osmoprotectant and a compatible solute; analysis of this exclusion yields a lower bound on the hydration of anionic protein carboxylate surface of two layers of water (>or=0.22 H(2)O A(-)(2)).

Authors+Show Affiliations

Department of Biochemistry, Program in Biophysics, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

15544344

Citation

Felitsky, Daniel J., et al. "The Exclusion of Glycine Betaine From Anionic Biopolymer Surface: Why Glycine Betaine Is an Effective Osmoprotectant but Also a Compatible Solute." Biochemistry, vol. 43, no. 46, 2004, pp. 14732-43.
Felitsky DJ, Cannon JG, Capp MW, et al. The exclusion of glycine betaine from anionic biopolymer surface: why glycine betaine is an effective osmoprotectant but also a compatible solute. Biochemistry. 2004;43(46):14732-43.
Felitsky, D. J., Cannon, J. G., Capp, M. W., Hong, J., Van Wynsberghe, A. W., Anderson, C. F., & Record, M. T. (2004). The exclusion of glycine betaine from anionic biopolymer surface: why glycine betaine is an effective osmoprotectant but also a compatible solute. Biochemistry, 43(46), 14732-43.
Felitsky DJ, et al. The Exclusion of Glycine Betaine From Anionic Biopolymer Surface: Why Glycine Betaine Is an Effective Osmoprotectant but Also a Compatible Solute. Biochemistry. 2004 Nov 23;43(46):14732-43. PubMed PMID: 15544344.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The exclusion of glycine betaine from anionic biopolymer surface: why glycine betaine is an effective osmoprotectant but also a compatible solute. AU - Felitsky,Daniel J, AU - Cannon,Jonathan G, AU - Capp,Michael W, AU - Hong,Jiang, AU - Van Wynsberghe,Adam W, AU - Anderson,Charles F, AU - Record,M Thomas,Jr PY - 2004/11/17/pubmed PY - 2005/1/19/medline PY - 2004/11/17/entrez SP - 14732 EP - 43 JF - Biochemistry JO - Biochemistry VL - 43 IS - 46 N2 - Paradoxically, glycine betaine (N,N,N-trimethyl glycine; GB) in vivo is both an effective osmoprotectant (efficient at increasing cytoplasmic osmolality and growth rate) and a compatible solute (without deleterious effects on biopolymer function, including stability and activity). For GB to be an effective osmoprotectant but not greatly affect biopolymer stability, we predict that it must interact very differently with folded protein surface than with that exposed in unfolding. To test this hypothesis, we quantify the preferential interaction of GB with the relatively uncharged surface exposed in unfolding the marginally stable lacI helix-turn-helix (HTH) DNA binding domain using circular dichroism and with the more highly charged surfaces of folded hen egg white lysozyme (HEWL) and bovine serum albumin (BSA) using all-gravimetric vapor pressure osmometry (VPO) and compare these results with results of VPO studies (Hong et al. (2004), Biochemistry, 43, 14744-14758) of the interaction of GB with polyanionic duplex DNA. For these four biopolymer surfaces, we observe that the extent of exclusion of GB per unit of biopolymer surface area increases strongly with increasing fraction of anionic oxygen (protein carboxylate or DNA phosphate) surface. In addition, GB is somewhat more excluded from the surface exposed in unfolding the lacI HTH and from the folded surface of HEWL than expected from their small fraction of anionic surface, consistent with moderate exclusion of GB from polar amide surface, as predicted by the osmophobic model of protein stability (Bolen and Baskakov (2001) J. Mol. Biol. 310, 955-963). Strong exclusion of GB from anionic surface explains how it can be both an effective osmoprotectant and a compatible solute; analysis of this exclusion yields a lower bound on the hydration of anionic protein carboxylate surface of two layers of water (>or=0.22 H(2)O A(-)(2)). SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/15544344/The_exclusion_of_glycine_betaine_from_anionic_biopolymer_surface:_why_glycine_betaine_is_an_effective_osmoprotectant_but_also_a_compatible_solute_ L2 - https://doi.org/10.1021/bi049115w DB - PRIME DP - Unbound Medicine ER -