Editing Stop codon (section)

=== Recognition ===
Recognition of stop codons in bacteria have been associated with the so-called 'tripeptide anticodon',<ref>{{cite journal |doi=10.1038/35001115 |title= A tripeptide 'anticodon' deciphers stop codons in messenger RNA |year=1999 |last1=Ito|first1=Koichi |last2= Uno|first2=Makiko |last3=Nakamura|first3=Yoshikazu |journal=Nature |volume=403 |issue= 6770 |pages= 680–4 |pmid=10688208 |s2cid= 4331695 }}</ref> a highly conserved amino acid motif in RF1 (PxT) and RF2 (SPF). Even though this is supported by structural studies, it was shown that the tripeptide anticodon hypothesis is an oversimplification.<ref>{{cite journal |doi=10.1074/jbc.M117.785238 |title= R213I mutation in release factor 2 (RF2) is one step forward for engineering an omnipotent release factor in bacteria ''Escherichia coli''|year=2017 |last1=Korkmaz|first1=Gürkan |last2= Sanyal|first2=Suparna |journal=Journal of Biological Chemistry|volume=292 |issue= 36|pages= 15134–42|pmid=28743745 |pmc=5592688|doi-access= free}}</ref>