Macrocyclization by asparaginyl endopeptidases

Research output: Contribution to journalReview article

6 Citations (Scopus)
31 Downloads (Pure)

Abstract

Plant asparaginyl endopeptidases (AEPs) are important for the post-translational processing of seed storage proteins via cleavage of precursor proteins. Some AEPs also function as peptide bond-makers during the biosynthesis of several unrelated classes of cyclic peptides, namely the kalata-type cyclic peptides, PawS-Derived Peptides and cyclic knottins. These three families of gene-encoded peptides have different evolutionary origins, but all have recruited AEPs for their maturation. In the last few years, the field has advanced rapidly, with the biochemical characterization of three plant AEPs capable of peptide macrocyclization, and insights have been gained from the first AEP crystal structures, albeit mammalian ones. Although the biochemical studies have improved our understanding of the mechanism of action, the focus now is to understand what changes in AEP sequence and structure enable some plant AEPs to perform macrocyclization reactions.

Original languageEnglish
Pages (from-to)923-928
JournalNew Phytologist
Volume218
Issue number3
DOIs
Publication statusPublished - May 2018

Fingerprint

asparaginylendopeptidase
proteinases
Cyclic Peptides
peptides
cyclic peptides
Peptides
Cystine-Knot Miniproteins
Seed Storage Proteins
seed storage proteins
Protein Precursors
crystal structure
mechanism of action

Cite this

@article{b7a010cfdb25461cab5a1fd502f73b03,
title = "Macrocyclization by asparaginyl endopeptidases",
abstract = "Plant asparaginyl endopeptidases (AEPs) are important for the post-translational processing of seed storage proteins via cleavage of precursor proteins. Some AEPs also function as peptide bond-makers during the biosynthesis of several unrelated classes of cyclic peptides, namely the kalata-type cyclic peptides, PawS-Derived Peptides and cyclic knottins. These three families of gene-encoded peptides have different evolutionary origins, but all have recruited AEPs for their maturation. In the last few years, the field has advanced rapidly, with the biochemical characterization of three plant AEPs capable of peptide macrocyclization, and insights have been gained from the first AEP crystal structures, albeit mammalian ones. Although the biochemical studies have improved our understanding of the mechanism of action, the focus now is to understand what changes in AEP sequence and structure enable some plant AEPs to perform macrocyclization reactions.",
keywords = "Journal Article, Review",
author = "James, {Amy M.} and Joel Haywood and Mylne, {Joshua S}",
note = "{\circledC} 2017 The Authors New Phytologist {\circledC} 2017 New Phytologist Trust.",
year = "2018",
month = "5",
doi = "10.1111/nph.14511",
language = "English",
volume = "218",
pages = "923--928",
journal = "The New Phytologist",
issn = "0028-646X",
publisher = "John Wiley & Sons",
number = "3",

}

Macrocyclization by asparaginyl endopeptidases. / James, Amy M.; Haywood, Joel; Mylne, Joshua S.

In: New Phytologist, Vol. 218, No. 3, 05.2018, p. 923-928.

Research output: Contribution to journalReview article

TY - JOUR

T1 - Macrocyclization by asparaginyl endopeptidases

AU - James, Amy M.

AU - Haywood, Joel

AU - Mylne, Joshua S

N1 - © 2017 The Authors New Phytologist © 2017 New Phytologist Trust.

PY - 2018/5

Y1 - 2018/5

N2 - Plant asparaginyl endopeptidases (AEPs) are important for the post-translational processing of seed storage proteins via cleavage of precursor proteins. Some AEPs also function as peptide bond-makers during the biosynthesis of several unrelated classes of cyclic peptides, namely the kalata-type cyclic peptides, PawS-Derived Peptides and cyclic knottins. These three families of gene-encoded peptides have different evolutionary origins, but all have recruited AEPs for their maturation. In the last few years, the field has advanced rapidly, with the biochemical characterization of three plant AEPs capable of peptide macrocyclization, and insights have been gained from the first AEP crystal structures, albeit mammalian ones. Although the biochemical studies have improved our understanding of the mechanism of action, the focus now is to understand what changes in AEP sequence and structure enable some plant AEPs to perform macrocyclization reactions.

AB - Plant asparaginyl endopeptidases (AEPs) are important for the post-translational processing of seed storage proteins via cleavage of precursor proteins. Some AEPs also function as peptide bond-makers during the biosynthesis of several unrelated classes of cyclic peptides, namely the kalata-type cyclic peptides, PawS-Derived Peptides and cyclic knottins. These three families of gene-encoded peptides have different evolutionary origins, but all have recruited AEPs for their maturation. In the last few years, the field has advanced rapidly, with the biochemical characterization of three plant AEPs capable of peptide macrocyclization, and insights have been gained from the first AEP crystal structures, albeit mammalian ones. Although the biochemical studies have improved our understanding of the mechanism of action, the focus now is to understand what changes in AEP sequence and structure enable some plant AEPs to perform macrocyclization reactions.

KW - Journal Article

KW - Review

U2 - 10.1111/nph.14511

DO - 10.1111/nph.14511

M3 - Review article

VL - 218

SP - 923

EP - 928

JO - The New Phytologist

JF - The New Phytologist

SN - 0028-646X

IS - 3

ER -