Random coil conformation of a Gly/Ala-rich insert in IκBα excludes structural stabilization as the mechanism for protection against proteasomal degradation

Ainars Leonchiks; Edvards Liepinsh; Mikhail Barishev; Anatoly Sharipo; Maria G. Masucci; Gottfried Otting

doi:10.1016/S0014-5793(98)01488-4

Random coil conformation of a Gly/Ala-rich insert in IκBα excludes structural stabilization as the mechanism for protection against proteasomal degradation

Ainars Leonchiks, Edvards Liepinsh, Mikhail Barishev, Anatoly Sharipo, Maria G. Masucci, Gottfried Otting

Institute of Microbiology and Virology

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

17 Citations (Scopus)

Abstract

Peptide segments of multiple glycine and alanine residues prevent the proteolytic degradation of ubiquitinated proteins by the proteasome. The structure of a Gly/Ala-rich insert in IκBα was probed by nuclear magnetic resonance (NMR) spectroscopy, comparing IκBα samples with and without Gly/Ala-rich insert. Narrow ¹H-NMR resonances at chemical shifts indicative of random coil conformations were observed in the difference spectrum. circular dichroism (CD) measurements further confirm that the mechanism of protection against proteolytic degradation is not based on structural transition or stabilization caused by the Gly/Ala-rich segment. In addition, most of the N- and C-terminal residues outside the ankyrin repeats in wild-type IκBα were found to be flexibly disordered. Copyright (C) 1998 Federation of European Biochemical Societies.

Original language	English
Pages (from-to)	365-369
Number of pages	5
Journal	FEBS Letters
Volume	440
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(98)01488-4
Publication status	Published - 4 Dec 1998

Keywords*

Amino acid analysis
Gly/Ala-rich peptide
IκBα
Nuclear magnetic resonance
Random coil conformation

Field of Science*

1.6 Biological sciences

Publication Type*

1.1. Scientific article indexed in Web of Science and/or Scopus database

Access to Document

10.1016/S0014-5793(98)01488-4

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title = "Random coil conformation of a Gly/Ala-rich insert in IκBα excludes structural stabilization as the mechanism for protection against proteasomal degradation",

abstract = "Peptide segments of multiple glycine and alanine residues prevent the proteolytic degradation of ubiquitinated proteins by the proteasome. The structure of a Gly/Ala-rich insert in IκBα was probed by nuclear magnetic resonance (NMR) spectroscopy, comparing IκBα samples with and without Gly/Ala-rich insert. Narrow 1H-NMR resonances at chemical shifts indicative of random coil conformations were observed in the difference spectrum. circular dichroism (CD) measurements further confirm that the mechanism of protection against proteolytic degradation is not based on structural transition or stabilization caused by the Gly/Ala-rich segment. In addition, most of the N- and C-terminal residues outside the ankyrin repeats in wild-type IκBα were found to be flexibly disordered. Copyright (C) 1998 Federation of European Biochemical Societies.",

keywords = "Amino acid analysis, Gly/Ala-rich peptide, IκBα, Nuclear magnetic resonance, Random coil conformation",

author = "Ainars Leonchiks and Edvards Liepinsh and Mikhail Barishev and Anatoly Sharipo and Masucci, {Maria G.} and Gottfried Otting",

note = "Funding Information: We thank Patrik Andersson for help with CD measurements. This work was supported by grants from the Swedish Natural Science Research Council, the Swedish Cancer Society, the Petrus and Augusta Hedlunds Stiftelse, the Karolinska Institute and the European Commission Training and Mobility of Research program, Contract no. ERBFMRXCT960026. A.L. was partially supported by a fellowship from the Swedish Institute and he is a fellow of `Joint MSc/PhD Program between Medical Academy of Latvia (AML) and Karolinska Institutet (KAMP)'. Copyright: Copyright 2007 Elsevier B.V., All rights reserved.",

year = "1998",

month = dec,

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doi = "10.1016/S0014-5793(98)01488-4",

language = "English",

volume = "440",

pages = "365--369",

journal = "FEBS Letters",

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publisher = "John Wiley and Sons Inc.",

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T1 - Random coil conformation of a Gly/Ala-rich insert in IκBα excludes structural stabilization as the mechanism for protection against proteasomal degradation

AU - Leonchiks, Ainars

AU - Liepinsh, Edvards

AU - Barishev, Mikhail

AU - Sharipo, Anatoly

AU - Masucci, Maria G.

AU - Otting, Gottfried

N1 - Funding Information: We thank Patrik Andersson for help with CD measurements. This work was supported by grants from the Swedish Natural Science Research Council, the Swedish Cancer Society, the Petrus and Augusta Hedlunds Stiftelse, the Karolinska Institute and the European Commission Training and Mobility of Research program, Contract no. ERBFMRXCT960026. A.L. was partially supported by a fellowship from the Swedish Institute and he is a fellow of `Joint MSc/PhD Program between Medical Academy of Latvia (AML) and Karolinska Institutet (KAMP)'. Copyright: Copyright 2007 Elsevier B.V., All rights reserved.

PY - 1998/12/4

Y1 - 1998/12/4

N2 - Peptide segments of multiple glycine and alanine residues prevent the proteolytic degradation of ubiquitinated proteins by the proteasome. The structure of a Gly/Ala-rich insert in IκBα was probed by nuclear magnetic resonance (NMR) spectroscopy, comparing IκBα samples with and without Gly/Ala-rich insert. Narrow 1H-NMR resonances at chemical shifts indicative of random coil conformations were observed in the difference spectrum. circular dichroism (CD) measurements further confirm that the mechanism of protection against proteolytic degradation is not based on structural transition or stabilization caused by the Gly/Ala-rich segment. In addition, most of the N- and C-terminal residues outside the ankyrin repeats in wild-type IκBα were found to be flexibly disordered. Copyright (C) 1998 Federation of European Biochemical Societies.

AB - Peptide segments of multiple glycine and alanine residues prevent the proteolytic degradation of ubiquitinated proteins by the proteasome. The structure of a Gly/Ala-rich insert in IκBα was probed by nuclear magnetic resonance (NMR) spectroscopy, comparing IκBα samples with and without Gly/Ala-rich insert. Narrow 1H-NMR resonances at chemical shifts indicative of random coil conformations were observed in the difference spectrum. circular dichroism (CD) measurements further confirm that the mechanism of protection against proteolytic degradation is not based on structural transition or stabilization caused by the Gly/Ala-rich segment. In addition, most of the N- and C-terminal residues outside the ankyrin repeats in wild-type IκBα were found to be flexibly disordered. Copyright (C) 1998 Federation of European Biochemical Societies.

KW - Amino acid analysis

KW - Gly/Ala-rich peptide

KW - IκBα

KW - Nuclear magnetic resonance

KW - Random coil conformation

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U2 - 10.1016/S0014-5793(98)01488-4

DO - 10.1016/S0014-5793(98)01488-4

M3 - Article

C2 - 9872404

AN - SCOPUS:0032437713

SN - 0014-5793

VL - 440

SP - 365

EP - 369

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Random coil conformation of a Gly/Ala-rich insert in IκBα excludes structural stabilization as the mechanism for protection against proteasomal degradation

Abstract

Keywords*

Field of Science*

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