Literature DB >> 28960135

Amyloids and prions in plants: Facts and perspectives.

K S Antonets1,2, A A Nizhnikov1,2.   

Abstract

Amyloids represent protein fibrils that have highly ordered structure with unique physical and chemical properties. Amyloids have long been considered lethal pathogens that cause dozens of incurable diseases in humans and animals. Recent data show that amyloids may not only possess pathogenic properties but are also implicated in the essential biological processes in a variety of prokaryotes and eukaryotes. Functional amyloids have been identified in archaea, bacteria, fungi, and animals, including humans. Plants are one of the most poorly studied groups of organisms in the field of amyloid biology. Although amyloid properties have not been shown under native conditions for any plant protein, studies demonstrating amyloid properties for a set of plant proteins in vitro or in heterologous systems in vivo have been published in recent years. In this review, we systematize the data on the amyloidogenic proteins of plants and their functions and discuss the perspectives of identifying novel amyloids using bioinformatic and proteomic approaches.

Entities:  

Keywords:  A. thaliana; AFP; Amyloid; LD; PSIA; S. cerevisiae; SARP; WALTZ; plant; prion; yeast

Mesh:

Substances:

Year:  2017        PMID: 28960135      PMCID: PMC5639834          DOI: 10.1080/19336896.2017.1377875

Source DB:  PubMed          Journal:  Prion        ISSN: 1933-6896            Impact factor:   3.931


  89 in total

1.  Amyloid-like aggregates of a plant protein: a case of a sweet-tasting protein, monellin.

Authors:  T Konno; K Murata; K Nagayama
Journal:  FEBS Lett       Date:  1999-07-02       Impact factor: 4.124

2.  Critical role of amyloid-like oligomers of Drosophila Orb2 in the persistence of memory.

Authors:  Amitabha Majumdar; Wanda Colón Cesario; Erica White-Grindley; Huoqing Jiang; Fengzhen Ren; Mohammed Repon Khan; Liying Li; Edward Man-Lik Choi; Kasthuri Kannan; Fengli Guo; Jay Unruh; Brian Slaughter; Kausik Si
Journal:  Cell       Date:  2012-01-26       Impact factor: 41.582

3.  Fibril formation from pea protein and subsequent gel formation.

Authors:  Claire Darizu Munialo; Anneke H Martin; Erik van der Linden; Harmen H J de Jongh
Journal:  J Agric Food Chem       Date:  2014-03-05       Impact factor: 5.279

4.  X-ray diffraction studies on amyloid filaments.

Authors:  E D Eanes; G G Glenner
Journal:  J Histochem Cytochem       Date:  1968-11       Impact factor: 2.479

5.  Isolation of low-molecular-weight proteins from amyloid plaque fibers in Alzheimer's disease.

Authors:  D J Selkoe; C R Abraham; M B Podlisny; L K Duffy
Journal:  J Neurochem       Date:  1986-06       Impact factor: 5.372

6.  A yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stress.

Authors:  Genjiro Suzuki; Naoyuki Shimazu; Motomasa Tanaka
Journal:  Science       Date:  2012-04-20       Impact factor: 47.728

7.  A radish seed antifungal peptide with a high amyloid fibril-forming propensity.

Authors:  Megan Garvey; Sarah Meehan; Sally L Gras; Horst J Schirra; David J Craik; Nicole L Van der Weerden; Marilyn A Anderson; Juliet A Gerrard; John A Carver
Journal:  Biochim Biophys Acta       Date:  2013-05-09

8.  A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in aplysia.

Authors:  Kausik Si; Maurizio Giustetto; Amit Etkin; Ruby Hsu; Agnieszka M Janisiewicz; Maria Conchetta Miniaci; Joung-Hun Kim; Huixiang Zhu; Eric R Kandel
Journal:  Cell       Date:  2003-12-26       Impact factor: 41.582

9.  Functional amyloid formation within mammalian tissue.

Authors:  Douglas M Fowler; Atanas V Koulov; Christelle Alory-Jost; Michael S Marks; William E Balch; Jeffery W Kelly
Journal:  PLoS Biol       Date:  2006-01       Impact factor: 8.029

Review 10.  Plant antimicrobial peptides.

Authors:  Robert Nawrot; Jakub Barylski; Grzegorz Nowicki; Justyna Broniarczyk; Waldemar Buchwald; Anna Goździcka-Józefiak
Journal:  Folia Microbiol (Praha)       Date:  2013-10-04       Impact factor: 2.099

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  5 in total

Review 1.  Why Study Functional Amyloids? Lessons from the Repeat Domain of Pmel17.

Authors:  Ryan P McGlinchey; Jennifer C Lee
Journal:  J Mol Biol       Date:  2018-06-07       Impact factor: 5.469

Review 2.  Biomolecular Assemblies: Moving from Observation to Predictive Design.

Authors:  Corey J Wilson; Andreas S Bommarius; Julie A Champion; Yury O Chernoff; David G Lynn; Anant K Paravastu; Chen Liang; Ming-Chien Hsieh; Jennifer M Heemstra
Journal:  Chem Rev       Date:  2018-10-03       Impact factor: 60.622

3.  Universal and taxon-specific trends in protein sequences as a function of age.

Authors:  Jennifer E James; Sara M Willis; Paul G Nelson; Catherine Weibel; Luke J Kosinski; Joanna Masel
Journal:  Elife       Date:  2021-01-08       Impact factor: 8.140

4.  Predicting Amyloidogenic Proteins in the Proteomes of Plants.

Authors:  Kirill S Antonets; Anton A Nizhnikov
Journal:  Int J Mol Sci       Date:  2017-10-16       Impact factor: 5.923

5.  Rippled β-Sheet Formation by an Amyloid-β Fragment Indicates Expanded Scope of Sequence Space for Enantiomeric β-Sheet Peptide Coassembly.

Authors:  Jennifer M Urban; Janson Ho; Gavin Piester; Riqiang Fu; Bradley L Nilsson
Journal:  Molecules       Date:  2019-05-23       Impact factor: 4.411

  5 in total

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