Leptosphaeria rhodopsin: bacteriorhodopsin-like proton pump from a eukaryote.

نویسندگان

  • Stephen A Waschuk
  • Arandi G Bezerra
  • Lichi Shi
  • Leonid S Brown
چکیده

Bacteriorhodopsin-like proteins provide archaea and eubacteria with a unique bioenergetic pathway comprising light-driven transmembrane proton translocation by a single retinal-binding protein. Recently, homologous proteins were found to perform photosensory functions in lower eukaryotes, but no active ion transport by eukaryotic rhodopsins was detected. By demonstrating light-driven proton pumping in a fungal rhodopsin from Leptosphaeria maculans, we present a case of a retinal-based proton transporter from a eukaryote. This result implies that in addition to oxidative phosphorylation and chlorophyll photosynthesis, some lower eukaryotes may have retained the archaeal route of building an electrochemical transmembrane gradient of protons.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Prokaryotic proton pumping in eukaryotes

Stephen Waschuk et al. report that the fungus Leptosphaeria maculans possesses a rhodopsin protein able to translocate protons across membranes in response to light, a function thought to be unique to prokaryotes. Traditionally, respiration and chlorophyll-based photosynthesis are the two methods used by eukaryotes to create a proton gradient, whereas archaebacteria undergo retinal-based photos...

متن کامل

Photochemical characterization of a novel fungal rhodopsin from Phaeosphaeria nodorum.

Eukaryotic microbial rhodopsins are widespread bacteriorhodopsin-like proteins found in many lower eukaryotic groups including fungi. Many fungi contain multiple rhodopsins, some significantly diverged from the original bacteriorhodopsin template. Although few fungal rhodopsins have been studied biophysically, both fast-cycling light-driven proton pumps and slow-cycling photosensors have been f...

متن کامل

A microbial rhodopsin with a unique retinal composition shows both sensory rhodopsin II and bacteriorhodopsin-like properties.

Rhodopsins possess retinal chromophore surrounded by seven transmembrane α-helices, are widespread in prokaryotes and in eukaryotes, and can be utilized as optogenetic tools. Although rhodopsins work as distinctly different photoreceptors in various organisms, they can be roughly divided according to their two basic functions, light-energy conversion and light-signal transduction. In microbes, ...

متن کامل

A phylogenetically distinctive and extremely heat stable light-driven proton pump from the eubacterium Rubrobacter xylanophilus DSM 9941T

Rhodopsins are proteins that contain seven transmembrane domains with a chromophore retinal and that function as photoreceptors for light-energy conversion and light-signal transduction in a wide variety of organisms. Here we characterized a phylogenetically distinctive new rhodopsin from the thermophilic eubacterium Rubrobacter xylanophilus DSM 9941T that was isolated from thermally polluted w...

متن کامل

Electrophysiological characterization of specific interactions between bacterial sensory rhodopsins and their transducers.

The halobacterial phototaxis receptors sensory rhodopsin I and II (SRI, SRII) enable the bacteria to seek optimal light conditions for ion pumping by bacteriorhodopsin and/or halorhodopsin. The incoming signal is transferred across the plasma membrane by means of receptor-specific transducer proteins that bind tightly to their corresponding photoreceptors. To investigate the receptor/transducer...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Proceedings of the National Academy of Sciences of the United States of America

دوره 102 19  شماره 

صفحات  -

تاریخ انتشار 2005