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Protein splicing control

DNA contains numerous other protein binding sites which are not palindromes but whose sequences represent additional encoded information. The RNA transcripts likewise contain sequences that direct the catalytic machinery involved in splicing, that bind to ribosomal proteins, that control rates of transcription, and that cause termination of transcription. [Pg.239]

Southworth MW, Adam E, Panne D, Byer R, Kautz R, Perler EB. Control of protein splicing by intein fragment reassembly. EMBO J. 1998 17(4) 918-926. [Pg.1793]

The possibility to identify and quantify protein-splicing variants by mass spectrometry has certainly attracted great interest from researchers in recent years, due to their variety of biological functions and their importance in many health- and disease-related processes. However, database searches are not yet optimized, and the ability to find a balance between the inclusion of all putative proteoform sequences (163) and the reduction of database size to control sequence redundancy and false-positives will definitely determine the success of this approach. [Pg.402]

Mootz HD, Blum ES, Tyszkiewicz AB, Muir TW (2003) Conditional protein splicing a new tool to control protein structure and function in vitro and in vivo. J Am Chem Soc 125 10561-10569... [Pg.219]

HDAC9 is the predominant member of the class II HDAC family expressed in heart (Zhang et al, 2002). Its major product was shown to encode the splice variant MEF2-interacting transcription repressor/histone deacetylase-related protein (MITRIHDRP), which lacks the enzymatic domain but forms complexes with both HDACI and HDAC3 (Zhou et al, 2000 Zhou et al, 2001) and has been recently implicated in skeletal muscle chromatin acetylation and gene expression under motor innervation control (Mejat et al, 2005). [Pg.268]


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Control proteins

Protein-splicing

SPLICE

Splicing

Splicing Control

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