Characterization of Escherichia coli 50S ribosomal protein L31

• Published in: FEMS microbiology letters Vol. 180; no. 2; pp. 345 - 349
• Main Authors: Eistetter, Anthony J., Butler, Peter D., Traut, Robert R., Fanning, Thomas G.
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 15.11.1999
• Subjects: Escherichia coli; Protein isolation; Protein modification; ribosomal protein L31; Ribosome; Ribosome; Protein isolation; Protein modification
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1016/S0378-1097(99)00505-4

The published C-terminal sequence of Escherichia coli 50S ribosomal protein L31, …RFNK (Brosius, J. (1978) Biochemistry 17, 501–508), differs from that predicted by the gene sequence, …RFNKRFNIPGSK (GenBank accession no. X78541). This discrepancy might be due to post-translational processing of the protein. To examine this possibility, we have isolated L31 from E. coli strain MRE600 and sequenced the C-terminal tryptic peptide. We find the sequence to be FBIPGSK. Size comparisons of L31 from several E. coli strains demonstrate that all are identical in size to the protein isolated from MRE600 and larger than the previously described protein, indicating that …RFNKRFNIPGSK represents the true C-terminus of L31. In addition, we show that the failure to identify L31 in many ribosome preparations is probably due to the protein’s loose association with the ribosome and its ability to form various intramolecular disulfide bonds, leading to L31 forms with distinct mobilities in gels.