Recombinant protein sequences can trigger methylation of N-terminal amino acids in Escherichia coli

Protein Science : a Publication of the Protein Society
I ApostolD Abbott-Brown

Abstract

Recombinant human hemoglobin rHb1.1 has been genetically engineered with the replacement of the wild-type valine residues at all N-termini with methionine, an Asn 108 Lys substitution on the beta globins, and a fusion of the two alpha globins with a glycine linker. When rHb1.1 was expressed in Escherichia coli, methylation of the N-terminal methionine of the alpha globin was discovered. Another mutant has been engineered with the alpha globin gene coding for N-terminal methionine followed by an insertion of alanine. Characterization of expressed hemoglobin from this variant revealed a methylated N-terminal alanine that occurred through two posttranslational events: initial excision of the N-terminal methionine, followed by methylation of alanine as the newly generated N-terminus. No methylation was observed for variants expressed with wild-type valine at the N-terminus of the alpha globin. The methylation of N-terminal amino acids was attributed to a specific protein sequence that can trigger methylation of proteins expressed in E. coli. Here we demonstrate that proline at position 4 in the protein sequence of alpha globin seems an essential part of that signaling. Although N-terminal methylation has been observed previously fo...Continue Reading

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Citations

Aug 1, 1996·Current Opinion in Structural Biology·K E SandersS Sligar
Jun 19, 2009·The Journal of Biological Chemistry·Véronique SauvéBen C Berks
May 7, 2015·ACS Chemical Biology·Byeong Sung LeeTae Hyeon Yoo
Apr 15, 2006·American Journal of Physiology. Regulatory, Integrative and Comparative Physiology·Korami DembeleB L Grégoire Nyomba
Dec 28, 2019·The Journal of Steroid Biochemistry and Molecular Biology·Katarzyna Sołtys, Andrzej Ożyhar

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