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Pentatricopeptide repeat proteins in plants
Barkan, Alice ; Small, Ian
Annual review of plant biology, 2014-01, Vol.65 (1), p.415-442
[Periódico revisado por pares]
United States: Annual Reviews, Inc
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Título:
Pentatricopeptide repeat proteins in plants
Autor:
Barkan, Alice
;
Small, Ian
Assuntos:
Amino Acid Sequence
;
Arabidopsis Proteins - chemistry
;
Arabidopsis Proteins - genetics
;
Arabidopsis Proteins - metabolism
;
Base Sequence
;
Flowers & plants
;
Models, Molecular
;
Molecular Sequence Data
;
Peptides
;
Photosynthesis
;
Plant Proteins - chemistry
;
Plant Proteins - genetics
;
Plant Proteins - metabolism
;
Plants - genetics
;
Plants - metabolism
;
Protein Structure, Secondary
;
Proteins
;
Repetitive Sequences, Amino Acid
;
Ribonucleic acid
;
RNA
;
RNA, Plant - chemistry
;
RNA, Plant - genetics
;
RNA, Plant - metabolism
;
RNA-Binding Proteins - genetics
;
RNA-Binding Proteins - metabolism
É parte de:
Annual review of plant biology, 2014-01, Vol.65 (1), p.415-442
Notas:
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-2
Descrição:
Pentatricopeptide repeat (PPR) proteins constitute one of the largest protein families in land plants, with more than 400 members in most species. Over the past decade, much has been learned about the molecular functions of these proteins, where they act in the cell, and what physiological roles they play during plant growth and development. A typical PPR protein is targeted to mitochondria or chloroplasts, binds one or several organellar transcripts, and influences their expression by altering RNA sequence, turnover, processing, or translation. Their combined action has profound effects on organelle biogenesis and function and, consequently, on photosynthesis, respiration, plant development, and environmental responses. Recent breakthroughs in understanding how PPR proteins recognize RNA sequences through modular base-specific contacts will help match proteins to potential binding sites and provide a pathway toward designing synthetic RNA-binding proteins aimed at desired targets.
Editor:
United States: Annual Reviews, Inc
Idioma:
Inglês
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