An Intrahelical Salt Bridge within the Trigger Site Stabilizes the GCN4 Leucine Zipper

Richard Kammerer; Richard A. Kammerer; Victor A. Jaravine; Sabine Frank; Therese Schulthess; Ruth Landwehr; Ariel Lustig; Carlos García-Echeverría; Andrei T. Alexandrescu; Jürgen Engel; Michel O. Steinmetz

An Intrahelical Salt Bridge within the Trigger Site Stabilizes the GCN4 Leucine Zipper

Richard Kammerer, Richard A. Kammerer, Victor A. Jaravine, Sabine Frank, Therese Schulthess, Ruth Landwehr, Ariel Lustig, Carlos García-Echeverría, Andrei T. Alexandrescu, Jürgen Engel, Michel O. Steinmetz

Research output: Contribution to journal › Article › peer-review

Abstract

We previously reported that a helical trigger segment within the GCN4 leucine zipper monomer is indispensable for the formation of its parallel two-stranded coiled coil. Here, we demonstrate that the intrinsic secondary structure of the trigger site is largely stabilized by an intrahelical salt bridge. Removal of this surface salt bridge by a single amino acid mutation induced only minor changes in the backbone structure of the GCN4 leucine zipper dimer as verified by nuclear magnetic resonance. The mutation, however, substantially destabilized the dimeric structure. These findings support the proposed hierarchic folding mechanism of the GCN4 coiled coil in which local helix formation within the trigger segment precedes dimerization.

Original language	English
Pages (from-to)	13685-13688
Number of pages	3
Journal	Journal of Biological Chemistry
Volume	276
Issue number	17
Publication status	Published - 27 Apr 2001

Cite this

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title = "An Intrahelical Salt Bridge within the Trigger Site Stabilizes the GCN4 Leucine Zipper",

abstract = "We previously reported that a helical trigger segment within the GCN4 leucine zipper monomer is indispensable for the formation of its parallel two-stranded coiled coil. Here, we demonstrate that the intrinsic secondary structure of the trigger site is largely stabilized by an intrahelical salt bridge. Removal of this surface salt bridge by a single amino acid mutation induced only minor changes in the backbone structure of the GCN4 leucine zipper dimer as verified by nuclear magnetic resonance. The mutation, however, substantially destabilized the dimeric structure. These findings support the proposed hierarchic folding mechanism of the GCN4 coiled coil in which local helix formation within the trigger segment precedes dimerization.",

author = "Richard Kammerer and Kammerer, {Richard A.} and Jaravine, {Victor A.} and Sabine Frank and Therese Schulthess and Ruth Landwehr and Ariel Lustig and Carlos Garc{\'i}a-Echeverr{\'i}a and Alexandrescu, {Andrei T.} and J{\"u}rgen Engel and Steinmetz, {Michel O.}",

year = "2001",

month = apr,

day = "27",

language = "English",

volume = "276",

pages = "13685--13688",

journal = "Journal of Biological Chemistry",

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T1 - An Intrahelical Salt Bridge within the Trigger Site Stabilizes the GCN4 Leucine Zipper

AU - Kammerer, Richard

AU - Kammerer, Richard A.

AU - Jaravine, Victor A.

AU - Frank, Sabine

AU - Schulthess, Therese

AU - Landwehr, Ruth

AU - Lustig, Ariel

AU - García-Echeverría, Carlos

AU - Alexandrescu, Andrei T.

AU - Engel, Jürgen

AU - Steinmetz, Michel O.

PY - 2001/4/27

Y1 - 2001/4/27

N2 - We previously reported that a helical trigger segment within the GCN4 leucine zipper monomer is indispensable for the formation of its parallel two-stranded coiled coil. Here, we demonstrate that the intrinsic secondary structure of the trigger site is largely stabilized by an intrahelical salt bridge. Removal of this surface salt bridge by a single amino acid mutation induced only minor changes in the backbone structure of the GCN4 leucine zipper dimer as verified by nuclear magnetic resonance. The mutation, however, substantially destabilized the dimeric structure. These findings support the proposed hierarchic folding mechanism of the GCN4 coiled coil in which local helix formation within the trigger segment precedes dimerization.

AB - We previously reported that a helical trigger segment within the GCN4 leucine zipper monomer is indispensable for the formation of its parallel two-stranded coiled coil. Here, we demonstrate that the intrinsic secondary structure of the trigger site is largely stabilized by an intrahelical salt bridge. Removal of this surface salt bridge by a single amino acid mutation induced only minor changes in the backbone structure of the GCN4 leucine zipper dimer as verified by nuclear magnetic resonance. The mutation, however, substantially destabilized the dimeric structure. These findings support the proposed hierarchic folding mechanism of the GCN4 coiled coil in which local helix formation within the trigger segment precedes dimerization.

M3 - Article

C2 - 11134036

SN - 1083-351X

VL - 276

SP - 13685

EP - 13688

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 17

ER -

An Intrahelical Salt Bridge within the Trigger Site Stabilizes the GCN4 Leucine Zipper

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