Sandbox WWC7: Difference between revisions

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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 thought to assist in RNA editing,<ref>PMID:17015439</ref> translation,<ref name = "translation">DOI:10.1073/pnas.1012076108</ref> and organelle biogenesis.<ref>PMID:15269332</ref> ~~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 <scene name='69/696301/Hairpins/1'>hairpins</scene>. These hairpin structures accumulate to form a α-solenoid tertiary structure. PPR proteins 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 (shown to the right) is a well-characterized P-class PPR protein found in the chloroplast of ''Zea mays'' which is often used as a model PPR protein.<ref name = "translation"/>

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 thought to assist in RNA editing,<ref>PMID:17015439</ref> translation,<ref name = "translation">DOI:10.1073/pnas.1012076108</ref> and organelle biogenesis.<ref>PMID:15269332</ref> While PPR proteins are found in many eukaryotes, 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 <scene name='69/696301/Hairpins/1'>hairpins</scene>. These hairpin structures accumulate to form a α-solenoid tertiary structure. PPR proteins 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 (shown to the right) is a well-characterized P-class PPR protein found in the chloroplast of ''Zea mays'' which is often used as a model PPR protein.<ref name = "translation"/>

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==Synthetic Applications==

~~There is~~ potential. ~~. .~~

Recent advances in programmable site-directed DNA-binding proteins (such as CRISPR/Cas9) have shown incredible potential for medical, agricultural, and scientific application. As a result, it is not surprising that

==References==

Sandbox WWC7: Difference between revisions

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-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 thought to assist in RNA editing,<ref>PMID:17015439</ref> translation,<ref name = "translation">DOI:10.1073/pnas.1012076108</ref> and organelle biogenesis.<ref>PMID:15269332</ref> 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 <scene name='69/696301/Hairpins/1'>hairpins</scene>. These hairpin structures accumulate to form a α-solenoid tertiary structure. PPR proteins 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 (shown to the right) is a well-characterized P-class PPR protein found in the chloroplast of ''Zea mays'' which is often used as a model PPR protein.<ref name = "translation"/>
+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 thought to assist in RNA editing,<ref>PMID:17015439</ref> translation,<ref name = "translation">DOI:10.1073/pnas.1012076108</ref> and organelle biogenesis.<ref>PMID:15269332</ref> While PPR proteins are found in many eukaryotes, 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 <scene name='69/696301/Hairpins/1'>hairpins</scene>. These hairpin structures accumulate to form a α-solenoid tertiary structure. PPR proteins 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 (shown to the right) is a well-characterized P-class PPR protein found in the chloroplast of ''Zea mays'' which is often used as a model PPR protein.<ref name = "translation"/>
 <Structure load='4OE1' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
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 ==Synthetic Applications==
-There is potential. . .
+Recent advances in programmable site-directed DNA-binding proteins (such as CRISPR/Cas9) have shown incredible potential for medical, agricultural, and scientific application. As a result, it is not surprising that
 ==References==
 {{Reflist}}