Add like
Add dislike
Add to saved papers

The role of FtsH complexes in the response to abiotic stress in cyanobacteria.

FtsH proteases (FtsHs) belong to intramembrane ATP-dependent metalloproteases which are widely distributed in eubacteria, mitochondria, and chloroplasts. The best studied role of FtsH in Escherichia coli includes quality control of membrane proteins, regulation of response to heat shock, superoxide stress and viral infection, and control of lipopolysaccharide biosynthesis. While heterotrophic bacteria mostly contain a single indispensable FtsH complex, the photosynthetic cyanobacteria usually contain three FtsH complexes: two heterocomplexes and one homocomplex. The essential cytoplasmic FtsH1/3 most probably fulfils a role similar to other bacterial FtsHs whereas the thylakoid FtsH2/3 heterocomplex and FtsH4 homocomplex appear to maintain the photosynthetic apparatus of cyanobacteria and optimize its functionality. Moreover, recent studies suggested involvement of all FtsH proteases in a complex response to nutrient stresses. In this review, we aim to comprehensively review the functions of the cyanobacterial FtsH complexes specifically under stress conditions with emphasis on nutrient deficiency and high irradiance. We also point to various unresolved issues concerning the FtsH functions, which deserve further attention.

Full text links

We have located open access text paper links.

Related Resources

For the best experience, use the Read mobile app

Mobile app image

Get seemless 1-tap access through your institution/university

For the best experience, use the Read mobile app

All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.

By using this service, you agree to our terms of use and privacy policy.

Your Privacy Choices Toggle icon

You can now claim free CME credits for this literature searchClaim now

Get seemless 1-tap access through your institution/university

For the best experience, use the Read mobile app