Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification

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Standard

Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification. / Lindorff-Larsen, Kresten; Lerche, Mathilde H.; Poulsen, Flemming Martin; Roepstorff, Peter; Winther, Jakob R.

I: Journal of Biological Chemistry, Bind 276, Nr. 36, 2001, s. 33547-53.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Lindorff-Larsen, K, Lerche, MH, Poulsen, FM, Roepstorff, P & Winther, JR 2001, 'Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification', Journal of Biological Chemistry, bind 276, nr. 36, s. 33547-53. https://doi.org/10.1074/jbc.M104841200

APA

Lindorff-Larsen, K., Lerche, M. H., Poulsen, F. M., Roepstorff, P., & Winther, J. R. (2001). Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification. Journal of Biological Chemistry, 276(36), 33547-53. https://doi.org/10.1074/jbc.M104841200

Vancouver

Lindorff-Larsen K, Lerche MH, Poulsen FM, Roepstorff P, Winther JR. Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification. Journal of Biological Chemistry. 2001;276(36):33547-53. https://doi.org/10.1074/jbc.M104841200

Author

Lindorff-Larsen, Kresten ; Lerche, Mathilde H. ; Poulsen, Flemming Martin ; Roepstorff, Peter ; Winther, Jakob R. / Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification. I: Journal of Biological Chemistry. 2001 ; Bind 276, Nr. 36. s. 33547-53.

Bibtex

@article{3ab341cee64a4bb49fb403440789e1f1,
title = "Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification",
abstract = "In plants a group of proteins termed nonspecific lipid transfer proteins are found. These proteins bind and catalyze transfer of lipids in vitro, but their in vivo function is unknown. They have been suggested to be involved in different aspects of plant physiology and cell biology, including the formation of cutin and involvement in stress and pathogen responses, but there is yet no direct demonstration of an in vivo function. We have found and characterized a novel post-translational modification of the barley nonspecific lipid transfer protein, LTP1. The protein-modification bond is of a new type in which an aspartic acid in LTP1 is bound to the modification through what most likely is an ester bond. The chemical structure of the modification has been characterized by means of two-dimensional homo- and heteronuclear nuclear magnetic resonance spectroscopy as well as mass spectrometry and is found to be lipid-like in nature. The modification does not resemble any standard lipid post-translational modification but is similar to a compound with known antimicrobial activity.",
author = "Kresten Lindorff-Larsen and Lerche, {Mathilde H.} and Poulsen, {Flemming Martin} and Peter Roepstorff and Winther, {Jakob R.}",
year = "2001",
doi = "10.1074/jbc.M104841200",
language = "English",
volume = "276",
pages = "33547--53",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "36",

}

RIS

TY - JOUR

T1 - Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification

AU - Lindorff-Larsen, Kresten

AU - Lerche, Mathilde H.

AU - Poulsen, Flemming Martin

AU - Roepstorff, Peter

AU - Winther, Jakob R.

PY - 2001

Y1 - 2001

N2 - In plants a group of proteins termed nonspecific lipid transfer proteins are found. These proteins bind and catalyze transfer of lipids in vitro, but their in vivo function is unknown. They have been suggested to be involved in different aspects of plant physiology and cell biology, including the formation of cutin and involvement in stress and pathogen responses, but there is yet no direct demonstration of an in vivo function. We have found and characterized a novel post-translational modification of the barley nonspecific lipid transfer protein, LTP1. The protein-modification bond is of a new type in which an aspartic acid in LTP1 is bound to the modification through what most likely is an ester bond. The chemical structure of the modification has been characterized by means of two-dimensional homo- and heteronuclear nuclear magnetic resonance spectroscopy as well as mass spectrometry and is found to be lipid-like in nature. The modification does not resemble any standard lipid post-translational modification but is similar to a compound with known antimicrobial activity.

AB - In plants a group of proteins termed nonspecific lipid transfer proteins are found. These proteins bind and catalyze transfer of lipids in vitro, but their in vivo function is unknown. They have been suggested to be involved in different aspects of plant physiology and cell biology, including the formation of cutin and involvement in stress and pathogen responses, but there is yet no direct demonstration of an in vivo function. We have found and characterized a novel post-translational modification of the barley nonspecific lipid transfer protein, LTP1. The protein-modification bond is of a new type in which an aspartic acid in LTP1 is bound to the modification through what most likely is an ester bond. The chemical structure of the modification has been characterized by means of two-dimensional homo- and heteronuclear nuclear magnetic resonance spectroscopy as well as mass spectrometry and is found to be lipid-like in nature. The modification does not resemble any standard lipid post-translational modification but is similar to a compound with known antimicrobial activity.

U2 - 10.1074/jbc.M104841200

DO - 10.1074/jbc.M104841200

M3 - Journal article

C2 - 11435437

VL - 276

SP - 33547

EP - 33553

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 36

ER -

ID: 44291416