Can periplasmic proteins such class A beta-lactamase be secreted outside gram negative cell? The protein is supposed to be anchored in periplasm through inner membrane.
Can anyone has right explanation for this?
There are examples of proteins gaining functionality through mutations of signal peptides. One that comes to mind is IdiA that is intracellular targeted in cyanobacteria but is homologous to a periplasm located protein in other bacteria.
See paragraph on pg 42 of Michel, K.-P. & Pistorius, E. K. Adaptation of the photosynthetic electron transport chain in cyanobacteria to iron deficiency: The function of IdiA and IsiA. Physiol. Plant. 120, 36–50 (2004).
I'm not that familiar with your particular protein or organism but I would compare the signal peptide sequence and look to see if there are mutations in any membrane-anchoring or protein-protein interaction domains.
Not the best answer but hopefully it gives you something to start with.
Thank you Jonathan. I am a bit sure about the periplasmic beta-lactamases as the test suggest. They are secreted out somehow through external stimulus or for some other factors.
- Badges
- Science topic
- Similar topics
- Biological Science
- Genetics
- Genetic Analysis