Lasso Proteins—Unifying Cysteine Knots and Miniproteins

Complex lasso proteins are a recently identified class of biological compounds that are present in considerable fraction of proteins with disulfide bridges. In this work, we look at complex lasso proteins as a generalization of well-known cysteine knots and miniproteins (lasso peptides). In particul...

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Autores principales: Bartosz Ambroży Greń, Pawel Dabrowski-Tumanski, Wanda Niemyska, Joanna Ida Sulkowska
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Publicado: MDPI AG 2021
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Acceso en línea:https://doaj.org/article/467f55480cd4499fad788c704f888529
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spelling oai:doaj.org-article:467f55480cd4499fad788c704f8885292021-11-25T18:49:06ZLasso Proteins—Unifying Cysteine Knots and Miniproteins10.3390/polym132239882073-4360https://doaj.org/article/467f55480cd4499fad788c704f8885292021-11-01T00:00:00Zhttps://www.mdpi.com/2073-4360/13/22/3988https://doaj.org/toc/2073-4360Complex lasso proteins are a recently identified class of biological compounds that are present in considerable fraction of proteins with disulfide bridges. In this work, we look at complex lasso proteins as a generalization of well-known cysteine knots and miniproteins (lasso peptides). In particular, we show that complex lasso proteins with the same crucial topological features—cysteine knots and lasso peptides—are antimicrobial proteins, which suggests that they act as a molecular plug. Based on an analysis of the stability of the lasso piercing residue, we also introduce a method to determine which lasso motif is potentially functional. Using this method, we show that the lasso motif in antimicrobial proteins, as well in that in cytokines, is functionally relevant. We also study the evolution of lasso motifs, their conservation, and the usefulness of the lasso fingerprint, which extracts all topologically non-triviality concerning covalent loops. The work is completed by the presentation of extensive statistics on complex lasso proteins to analyze, in particular, the strange propensity for “negative” piercings. We also identify 21 previously unknown complex lasso proteins with an ester and a thioester bridge.Bartosz Ambroży GreńPawel Dabrowski-TumanskiWanda NiemyskaJoanna Ida SulkowskaMDPI AGarticletopologylassoproteinsOrganic chemistryQD241-441ENPolymers, Vol 13, Iss 3988, p 3988 (2021)
institution DOAJ
collection DOAJ
language EN
topic topology
lasso
proteins
Organic chemistry
QD241-441
spellingShingle topology
lasso
proteins
Organic chemistry
QD241-441
Bartosz Ambroży Greń
Pawel Dabrowski-Tumanski
Wanda Niemyska
Joanna Ida Sulkowska
Lasso Proteins—Unifying Cysteine Knots and Miniproteins
description Complex lasso proteins are a recently identified class of biological compounds that are present in considerable fraction of proteins with disulfide bridges. In this work, we look at complex lasso proteins as a generalization of well-known cysteine knots and miniproteins (lasso peptides). In particular, we show that complex lasso proteins with the same crucial topological features—cysteine knots and lasso peptides—are antimicrobial proteins, which suggests that they act as a molecular plug. Based on an analysis of the stability of the lasso piercing residue, we also introduce a method to determine which lasso motif is potentially functional. Using this method, we show that the lasso motif in antimicrobial proteins, as well in that in cytokines, is functionally relevant. We also study the evolution of lasso motifs, their conservation, and the usefulness of the lasso fingerprint, which extracts all topologically non-triviality concerning covalent loops. The work is completed by the presentation of extensive statistics on complex lasso proteins to analyze, in particular, the strange propensity for “negative” piercings. We also identify 21 previously unknown complex lasso proteins with an ester and a thioester bridge.
format article
author Bartosz Ambroży Greń
Pawel Dabrowski-Tumanski
Wanda Niemyska
Joanna Ida Sulkowska
author_facet Bartosz Ambroży Greń
Pawel Dabrowski-Tumanski
Wanda Niemyska
Joanna Ida Sulkowska
author_sort Bartosz Ambroży Greń
title Lasso Proteins—Unifying Cysteine Knots and Miniproteins
title_short Lasso Proteins—Unifying Cysteine Knots and Miniproteins
title_full Lasso Proteins—Unifying Cysteine Knots and Miniproteins
title_fullStr Lasso Proteins—Unifying Cysteine Knots and Miniproteins
title_full_unstemmed Lasso Proteins—Unifying Cysteine Knots and Miniproteins
title_sort lasso proteins—unifying cysteine knots and miniproteins
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/467f55480cd4499fad788c704f888529
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AT paweldabrowskitumanski lassoproteinsunifyingcysteineknotsandminiproteins
AT wandaniemyska lassoproteinsunifyingcysteineknotsandminiproteins
AT joannaidasulkowska lassoproteinsunifyingcysteineknotsandminiproteins
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