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Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro

Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro

Published on: May 3, 2014

Catalytic roles of the AMP at the 3' end of tRNAs

N S Wickramasinghe¹, J C Lacey

¹Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham 35294.

Molecular and Cellular Biochemistry

|October 26, 1994

Abstract:

Recent reports suggest that the ribosome retains considerable peptidyl transferase activity even when much of the protein of the ribosome is removed and further suggests that rRNA may be the peptidyl transferase. The work here suggests that the AMP residue at the 3' terminus of each tRNA has some catalytic activity both in the esterification reaction and in forming a pseudopeptide, AcGly, and further suggests that whatever peptidyl transferase is, it finds a cooperative substrate in the aminoacyl-AMP at the 3' terminus of tRNA.

Keywords:

NASA Discipline Exobiology Non-NASA Center

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