Disease relevance of N-formyl-L-methionine

• The entire amino acid sequence of rat liver fatty acid-binding protein along with an amino-terminal formyl-methionine was modeled in the crystal structure [1].
• Bacterial infection promotes the infiltration of inflammatory leukocytes mediated in part by receptors for formyl-methionine-terminated peptides [2].
• Antigenic mapping using two sera specific for the human initiator methionine tRNA revealed separate epitopes, one of which is conserved in formyl-methionine initiator tRNA from Escherichia coli [3].
• The size of the smaller fmet polypeptide synthesized in vitro by the defective virus appears identical in size to that of the standard virus [4].
• Although the identity of the small (5,000 to 10,000 daltons) fmet polypeptide is not clear, several lines of evidence enable us to exclude the possibility that it is VP4, the smallest viral capsid protein [4].

High impact information on N-formyl-L-methionine

• Analysis by partial proteolytic digestion of the P23 family labeled biosynthetically with [35S] methionine, and P23, labeled with [35S] formyl-methionine by in vitro translation of RNA from infected cells, revealed that the proteins of the P23 family differ in their amino-terminal domains [5].
• Both the standard virus and the defective-interfering virus RNA direct the synthesis of two polypeptides labeled with n-formyl-methionine (fmet) at their amino termini [4].
• Of interest, peptides containing formyl-methionine are potent chemoattractants for neutrophils, suggesting that delta-toxin deformylation may have functional consequences [6].
• The transition from producing both species of delta-toxin to producing only formyl-methionine-containing delta-toxin coincided with increased tricarboxylic acid (TCA) cycle activity [6].
• The low incorporation in comparison to formyl-methionine was not due to the lack of interaction of fluorophore-Met-tRNA(f) with IF-2 [7].

Anatomical context of N-formyl-L-methionine

• Bovine cornea extracted with 0.154 M NaCl yielded a protein fraction which (i) inhibited protein synthesis in rabbit reticulocyte lysates, and (ii) reduced the incorporation of formyl-methionine from f[35S]Met-tRNA(f) into polypeptides [8].

Associations of N-formyl-L-methionine with other chemical compounds

• The B800 BChl-as exhibit a different ligation from that of Rps. acidophila (aspartate is the Mg ligand as opposed to formyl-methionine in Rps. acidophila) [9].

Analytical, diagnostic and therapeutic context of N-formyl-L-methionine

• Amino-terminal sequence analysis and electrospray ionization mass spectrometry confirmed the identity of the thioesterase and revealed that the amino-terminal formyl-methionine had been removed yielding a subunit species of average molecular mass 31,842 Da [10].

References