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InterPro: IPR002885 Pentatricopeptide repeat
Protein matches
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UniProtKB Matches: 6131 proteins |
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Accession
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IPR002885 Pentatricopeptide_repeat |
Type
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Repeat |
Signatures
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InterPro annotation
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Entry Details in BioMart
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Abstract
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This entry represents the PPR repeat.
Pentatricopeptide repeat (PPR) proteins are characterised by tandem repeats of a degenerate 35 amino acid motif [1]. Most of PPR proteins have roles in mitochondria or plastid [2]. PPR repeats were discovered while screening Arabidopsis proteins for those predicted to be targeted to mitochondria or chloroplast [1, 3]. Some of these proteins have been shown to play a role in post-transcriptional processes within organelles and they are thought to be sequence-specific RNA-binding proteins [4, 5, 6]. Plant genomes have between one hundred to five hundred PPR genes per genome whereas non-plant genomes encode two to six PPR proteins.
Although no PPR structures are yet known, the motif is predicted to fold into a helix-turn-helix structure similar to those found in the tetratricopeptide repeat (TPR) family (see PDOC50005) [1].
The plant PPR protein family has been divided in two subfamilies on the basis of their motif content and organisation [3, 7].
Examples of PPR repeat-containing proteins include PET309 P32522, which may be involved in RNA stabilisation [8], and crp1, which is involved in RNA processing [9]. The repeat is associated with a predicted plant protein O49549 that has a domain organisation similar to the human BRCA1 protein.
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Database links
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Pfam Clan: CL0020.21
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Example proteins
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A3KPF8 Pentatricopeptide repeat-containing protein At1g79080, chloroplastic
O75064 DENN domain-containing protein 4B
P32522 Pentatricopeptide repeat-containing protein PET309, mitochondrial
Q14C51 Pentatricopeptide repeat-containing protein 3, mitochondrial
Q76C99 Protein Rf1, mitochondrial
More proteins
Example Proteins Key
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Publications
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1.
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Small ID, Peeters N.
The PPR motif - a TPR-related motif prevalent in plant organellar proteins.
Trends Biochem. Sci. 25 46-7 2000
[PubMed: 10664580]
http://dx.doi.org/10.1016/S0968-0004(99)01520-0
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2.
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Nakamura T, Schuster G, Sugiura M, Sugita M.
Chloroplast RNA-binding and pentatricopeptide repeat proteins.
Biochem. Soc. Trans. 32 571-4 2004
[PubMed: 15270678]
http://www.biochemsoctrans.org/bst/032/bst0320571.htm
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3.
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Lurin C, Andres C, Aubourg S, Bellaoui M, Bitton F, Bruyere C, Caboche M, Debast C, Gualberto J, Hoffmann B, Lecharny A, Le Ret M, Martin-Magniette ML, Mireau H, Peeters N, Renou JP, Szurek B, Taconnat L, Small I.
Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins reveals their essential role in organelle biogenesis.
Plant Cell 16 2089-103 2004
[PubMed: 15269332]
http://dx.doi.org/10.1105/tpc.104.022236
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4.
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Meierhoff K, Felder S, Nakamura T, Bechtold N, Schuster G.
HCF152, an Arabidopsis RNA binding pentatricopeptide repeat protein involved in the processing of chloroplast psbB-psbT-psbH-petB-petD RNAs.
Plant Cell 15 1480-95 2003
[PubMed: 12782738]
http://dx.doi.org/10.1105/tpc.010397
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5.
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Mili S, Pinol-Roma S.
LRP130, a pentatricopeptide motif protein with a noncanonical RNA-binding domain, is bound in vivo to mitochondrial and nuclear RNAs.
Mol. Cell. Biol. 23 4972-82 2003
[PubMed: 12832482]
http://dx.doi.org/10.1128/MCB.23.14.4972-4982.2003
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6.
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Delannoy E, Stanley WA, Bond CS, Small ID.
Pentatricopeptide repeat (PPR) proteins as sequence-specificity factors in post-transcriptional processes in organelles.
Biochem. Soc. Trans. 35 1643-7 2007
[PubMed: 18031283]
http://dx.doi.org/10.1042/BST0351643
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7.
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Saha D, Prasad AM, Srinivasan R.
Pentatricopeptide repeat proteins and their emerging roles in plants.
Plant Physiol. Biochem. 45 521-34 2007
[PubMed: 17560114]
http://dx.doi.org/10.1016/j.plaphy.2007.03.026
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8.
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Manthey GM, McEwen JE.
The product of the nuclear gene PET309 is required for translation of mature mRNA and stability or production of intron-containing RNAs derived from the mitochondrial COX1 locus of Saccharomyces cerevisiae.
EMBO J. 14 4031-43 1995
[PubMed: 7664742]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=7664742&action=stream&blobtype=pdf
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9.
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Barkan A, Walker M, Nolasco M, Johnson D.
A nuclear mutation in maize blocks the processing and translation of several chloroplast mRNAs and provides evidence for the differential translation of alternative mRNA forms.
EMBO J. 13 3170-81 1994
[PubMed: 8039510]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8039510&action=stream&blobtype=pdf
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InterPro 23.1
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