The control of transmembrane helix transverse position in membranes by hydrophilic residues.

The control of transmembrane helix transverse position in membranes by hydrophilic residues. Research Abstract Details 

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The control of transmembrane helix transverse position in membranes by hydrophilic residues. Abstract Text:

Shyam S Krishnakumar,Erwin London,Shyam S Krishnakumar,Erwin London,

The ability of hydrophilic residues to shift the transverse position of transmembrane (TM) helices within bilayers was studied in model membrane vesicles. Transverse shifts were detected by fluorescence measurements of the membrane depth of a Trp residue at the center of a hydrophobic sequence. They were also estimated from the effective length of the TM-spanning sequence, derived from the stability of the TM configuration under conditions of negative hydrophobic mismatch. Hydrophilic residues (at the fifth position in a 21-residue hydrophobic sequence composed of alternating Leu and Ala residues and flanked on both ends by two Lys) induced transverse shifts that moved the hydrophilic residue closer to the membrane surface. At pH 7, the dependence of the extent of shift upon the identity of the hydrophilic residue increased in the order: L < G approximately = Y approximately = T < R approximately = H < S < P < K < E approximately = Q < N < D. By varying pH, shifts with ionizable residues fully charged or uncharged were measured, and the extent of shift increased in the order: L < G approximately = Y approximately = H(o) approximately = T < E(o) approximately = R < S < P < K+ < Q approximately = D(o) approximately = H+ < N approximately = E- < D-. The dependence of transverse shifts upon hydrophilic residue identity was consistent with the hypothesis that shift magnitude is largely controlled by the combination of side chain hydrophilicity, ionization state, and ability to position polar groups near the bilayer surface (snorkeling). Additional experiments showed that shift was also modulated by the position of the hydrophilic residue in the sequence and the hydrophobicity of the sequence moved out of the bilayer core upon shifting. Combined, these studies show that the insertion boundaries of TM helices are very sensitive to sequence, and can be altered even by weakly hydrophilic residues. Thus, many TM helices may have the capacity to exist in more than one transverse position. Knowledge of the magnitudes of transverse shifts induced by different hydrophilic residues should be useful for design of mutagenesis studies measuring the effect of transverse TM helix position upon function.

The control of transmembrane helix transverse position in membranes by hydrophilic residues. Publishing Authors By Initials

SS Krishnakumar,E London,SS Krishnakumar,E London,

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The control of transmembrane helix transverse position in membranes by hydrophilic residues. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of molecular biology

VOLUME: 374

Page Numbers: 1251-69

Journal Abbreviation: J. Mol. Biol.

ISSN: 1089-8638

DAY: 17

MONTH: 10

YEAR: 2007

The control of transmembrane helix transverse position in membranes by hydrophilic residues. Information

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LANGUAGE: eng

NlmUniqueID: 2985088

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Grant and Affiliation Information for The control of transmembrane helix transverse position in membranes by hydrophilic residues.

AFFILIATION: Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.

Country: England

AGENCY: United States NHLBI

GRANT: HL63768

ACRONYM: HL

MEDLINETA: J Mol Biol

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