Sandbox WWC7
From Proteopedia
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| + | <Structure load='4m57' size='350' frame='true' align='right' caption='PPR10 structure isolated from ''Zea Mays'' (PDB code [[4m57]])' scene='Insert optional scene name here' /> | ||
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==Introduction== | ==Introduction== | ||
Pentatricopeptide repeat (PPR) proteins are a family of sequence specific RNA-binding proteins which participate in organelle RNA metabolism. Although the mechanisms of RNA binding and the functions of PPR proteins are not fully understood, PPR proteins are known to assist in RNA editing, and they make up the majority of RNA-binding factors in plant organelles. PPR proteins are characterized by a series of tandem-repeat amino acid consensus sequences which form α-helix hairpins, and they can belong to one of two classes: P-class and PLS-class, with the P-class containing 35 amino acid repeats and the PLS-class containing 31-36 amino acid repeats. PPR10 is a P-class PPR protein found in the chloroplast of ''Zea mays''. It binds specifically to the RNA oligonucleotides ATPH (17 nucleotides) and SPAJ (18 nucleotides). | Pentatricopeptide repeat (PPR) proteins are a family of sequence specific RNA-binding proteins which participate in organelle RNA metabolism. Although the mechanisms of RNA binding and the functions of PPR proteins are not fully understood, PPR proteins are known to assist in RNA editing, and they make up the majority of RNA-binding factors in plant organelles. PPR proteins are characterized by a series of tandem-repeat amino acid consensus sequences which form α-helix hairpins, and they can belong to one of two classes: P-class and PLS-class, with the P-class containing 35 amino acid repeats and the PLS-class containing 31-36 amino acid repeats. PPR10 is a P-class PPR protein found in the chloroplast of ''Zea mays''. It binds specifically to the RNA oligonucleotides ATPH (17 nucleotides) and SPAJ (18 nucleotides). | ||
Revision as of 16:29, 23 April 2016
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Introduction
Pentatricopeptide repeat (PPR) proteins are a family of sequence specific RNA-binding proteins which participate in organelle RNA metabolism. Although the mechanisms of RNA binding and the functions of PPR proteins are not fully understood, PPR proteins are known to assist in RNA editing, and they make up the majority of RNA-binding factors in plant organelles. PPR proteins are characterized by a series of tandem-repeat amino acid consensus sequences which form α-helix hairpins, and they can belong to one of two classes: P-class and PLS-class, with the P-class containing 35 amino acid repeats and the PLS-class containing 31-36 amino acid repeats. PPR10 is a P-class PPR protein found in the chloroplast of Zea mays. It binds specifically to the RNA oligonucleotides ATPH (17 nucleotides) and SPAJ (18 nucleotides).
