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

Protein Science

Volumn 4, Issue 12, 1995, Pages 2616-2618

  Apostol, Izydor ^a   Aitken, Jackie ^a   Levine, Joe ^a   Lippincott, Julie ^a   Davidson, Jeffrey S ^a   Abbott‐Brown, Debbie ^a  

^a BAXTER HEALTHCARE CORPORATION   (United States)

Author keywords

methylation signal; posttranslational modifications; recombinant human hemoglobin

Indexed keywords

HEMOGLOBIN; RECOMBINANT PROTEIN;

AMINO ACID COMPOSITION; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; ESCHERICHIA COLI; GENETIC ENGINEERING; HUMAN; METHYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PROCESSING;

ALANINE; AMINO ACID SEQUENCE; ESCHERICHIA COLI; HEMOGLOBINS; HUMAN; METHIONINE; METHYLATION; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; RECOMBINANT PROTEINS;

EID: 0028825194     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.5560041219     Document Type: Article

References (12)

1. The primary structure of protein L16 located at the peptidyltransferase center of Escherichia coli ribosomes
2. Occurrence of methylated amino acids as N‐termini of proteins from Escherichia coli ribosomes
3. Expression of fully functional tetrameric human hemoglobin in Escherichia coli
4. Extent of N‐terminal methionine excision from Escherichia coli proteins is governed by the side‐chain length of the penultimate amino acid
5. N‐terminal modification of malarial antigens from E. coli
6. A human recombinant haemoglobin designed for use as blood substitute
7. Expression of recombinant human hemoglobin in Escherichia coli
8. N‐methylmethionine at the amino terminus of a protein required for bacterial chemotaxis
9. N‐terminal methylation of proteins: Structure, function and specificity
10. A second type of proteins methylation reaction in bacterial chemotaxis
11. Bacterial chemotaxis and the molecular logic of intracellular signal transduction networks