Infection biology: The elusive third factor

Jun 22, 2012

Researchers from Ludwig-Maximilians-Universität (LMU) in Munich have identified an enzyme that is involved in a modification pathway that is essential for bacterial pathogenicity. Because it shows no similarity to other known proteins, it may be an ideal target for development of novel antimicrobial drugs.

Studies on a number of pathogenic bacteria have shown that these strains become pathogenic only when an called elongation factor P (EF-P) is chemically modified on a conserved lysine residue. EF-P is a universally conserved translation factor, which is involved in protein synthesis. Two enzymes are known to be involved in modifying the conserved lysine of EF-P, however these enzymes cannot fully account for the pattern of modification seen on EF-P in living cells.

The mystery molecule

Thus, at least one other protein must be involved in the modification process – however to date it has proved to be particularly elusive. Now a research team led by LMU biochemist Daniel Wilson, who is also affiliated with the Center for Integrated Protein Science Munich (CIPSM), a Cluster of Excellence at LMU, has succeeded in identifying the mystery protein as the enzyme YfcM and showing that it displays hydroxylase activity. Strikingly, YfcM shows no sequence similarity to any other known protein and therefore may have a unique structure.

This is not the only reason why discovery of YfcM will arouse great interest. "YfcM may turn out to be an ideal target for the development of new - and urgently needed – antibiotics, however more insight will be needed to ascertain the role of the YfcM mediated hydroxylation of EF-P," says Wilson.

Explore further: Environmental pollutants make worms susceptible to cold

add to favorites email to friend print save as pdf

Related Stories

Copycat protein finds a perfect match

Nov 19, 2010

As proteins are synthesized during messenger RNA translation, fresh amino acids are delivered to the ribosome of the cell by nucleic acid molecules known as transfer RNAs (tRNAs). Each amino acid has a cognate ...

Core tenets of the 'histone code' are universal

Sep 06, 2007

In one of biology’s most impressive engineering feats, specialized proteins called histones package some six-and-a-half feet of human DNA into a nucleus that averages just five microns in diameter.

Recommended for you

Environmental pollutants make worms susceptible to cold

12 hours ago

Some pollutants are more harmful in a cold climate than in a hot, because they affect the temperature sensitivity of certain organisms. Now researchers from Danish universities have demonstrated how this ...

A new quality control pathway in the cell

Sep 18, 2014

Proteins are important building blocks in our cells and each cell contains millions of different protein molecules. They are involved in everything from structural to regulatory aspects in the cell. Proteins are constructed ...

User comments : 0