Dead Sea-dwelling microbes reveal roots of protein common to all higher life forms

Jan 11, 2010 by Stu Hutson

(PhysOrg.com) -- We have more in common with Dead Sea-dwelling microbes than previously thought. University of Florida researchers have found that one of the most common proteins in complex life forms may have evolved from proteins found in microbes that live in deadly salty environments.

We have more in common with Dead Sea-dwelling than previously thought. University of Florida researchers have found that one of the most common proteins in complex life forms may have evolved from proteins found in microbes that live in deadly salty environments.

The protein ubiquitin is so-called because it is ubiquitously active in all higher life forms on Earth. The protein is essential to the life cycle of nearly all eukaryotic cells — those that are complex enough to have a nucleus and other membrane-bound structures.

Haloferax volcanii microbes, on the other hand, are unique creatures. One of the most on the planet, they long ago adapted to conditions far too salty for other organisms — even surviving for thousands of years in dried-out salt lakes.

As they report in the Jan. 7 issue of the journal Nature, researchers for UF’s Institute of Food and Agricultural Sciences have found that two proteins in Haloferax are likely the simple evolutionary precursors of ubiquitin.

These two proteins, dubbed SAMP1 and SAMP2, seem to perform similar functions to ubiquitin without some of enzymes that are needed for ubiquitin to function in eukaryotes, said Julie Maupin-Furlow, the study’s lead researcher and professor in UF’s department of microbiology and cell science.

The finding not only lends insight into how ubiquitin evolved, but it also reveals that this seemingly complex may have some simple mechanisms that can be examined for use as potential medical treatments, Maupin-Furlow said.

Researchers are currently investigating ’s role in a broad range of diseases such as cancer, , neurodegenerative disorders, muscle wasting, diabetes and various inflammatory conditions.

“This opens the door to a new avenue of study for this very important protein,” Maupin-Furlow said. “And it gives us a broader picture of some of the common aspects of life on Earth.”

Explore further: How plant cell compartments change with cell growth

Related Stories

Team finds most complex protein knot ever seen

Sep 20, 2006

An MIT team has discovered the most complicated knot ever seen in a protein, and they believe it may be linked to the protein's function as a rescue agent for proteins marked for destruction.

New protein identified in bacterial arsenal

Mar 03, 2009

(PhysOrg.com) -- Nearly a billion years ago, bacteria evolved an insidious means of infecting their hosts — a syringe-like mechanism able to inject cells with stealthy hijacker molecules. These molecules, ...

When proteins change partners

Sep 11, 2009

Dieter Wolf, M.D., and colleagues at Burnham Institute for Medical Research (Burnham) have illuminated how competition between proteins enhances combinatorial diversity during ubiquitination (the process that marks proteins ...

Researchers identify a scaffold regulating protein disposal

Dec 11, 2009

How does a cell manage to identify and degrade the diverse types of defective proteins and thus protect the body against serious diseases? The researchers Sabine C. Horn, Professor Thomas Sommer, Professor Udo Heinemann and ...

Recommended for you

How plant cell compartments change with cell growth

18 hours ago

A research team led by Kiminori Toyooka from the RIKEN Center for Sustainable Resource Science has developed a sophisticated microscopy technique that for the first time captures the detailed movement of ...

Plants can 'switch off' virus DNA

18 hours ago

A team of virologists and plant geneticists at Wageningen UR has demonstrated that when tomato plants contain Ty-1 resistance to the important Tomato yellow leaf curl virus (TYLCV), parts of the virus DNA ...

A better understanding of cell to cell communication

19 hours ago

Researchers of the ISREC Institute at the School of Life Sciences, EPFL, have deciphered the mechanism whereby some microRNAs are retained in the cell while others are secreted and delivered to neighboring ...

A glimpse at the rings that make cell division possible

19 hours ago

Forming like a blown smoke ring does, a "contractile ring" similar to a tiny muscle pinches yeast cells in two. The division of cells makes life possible, but the actual mechanics of this fundamental process ...

User comments : 0