Molecular recognition of mRNA 5′ cap by 3′ poly(A)-specific ribonuclease (PARN) differs from interactions known for other cap-binding proteins
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- 作者：Anna Niedzwieckaa ; annan@ifpan.edu.pl" class="auth_mail" title="E-mail the corresponding author ; Per Nilssonb ; 1 ; Remigiusz Worcha ; Janusz Stepinskic ; Edward Darzynkiewiczc ; d ; Anders Virtanenb
- 关键词：PARN ; poly(A)-specific ribonuclease ; eIF4E ; eukaryotic Initiation Factor 4E and similarly 4G ; 4 ; A factors ; 4E-BPs ; eIF4E binding proteins ; CBC ; Cap Binding Complex ; CBP20 ; Cap Binding Protein 20 ; m7GpppG ; P1-guanosine-5&prime ; P3-(7-methylguanosine-5&prime ; ) triphosphate ; m7Gpppm2&prime ; OG ; P1-(O2&prime ; -methylguanosine-5&prime ; ) P3-(7-methylguanosine-5&prime ; ) triphosphate ; GpppG ; P1 ; P3-bisguanosine-5&prime ; triphosphate ; m7GpppGLew&ndash ; EDA ; P1-7-methylguanosine-5&prime ; P3-{2&prime ; 3&p
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：April 2016
- 年：2016
- 卷：1864
- 期：4
- 页码：331-345
- 全文大小：1907 K
文摘
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5′ mRNA cap recognition by PARN is distinct from other known cap-binding proteins.
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Two cap-binding sites of the PARN dimer exhibit a negative cooperativity.
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Non-coulombic interactions are major factors in the PARN–cap interaction.
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Slow kinetics of assembly and dissociation provides stabilization of the complex.
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PARN has versatile activity toward alternative forms of the 5′ cap