科研人员提供生命起源的线索

A structural biologist at the Florida State University College of Medicine has made discoveries that could lead scientists a step closer to understanding how life first emerged on Earth billions of years ago. Professor Michael Blaber and his team produced data supporting the idea that 10 amino acids believed to exist on Earth around 4 billion years ago were capable of forming foldable proteins in a high-salt (halophile) environment. Such proteins would have been capable of providing metabolic activity for the first living organisms to emerge on the planet between 3.5 and 3.9 billion years ago.

The results of Blaber's three-year study, which was built around investigative techniques that took more than 17 years to develop, are published in the journal Proceedings of the National Academy of Sciences.

The first living organisms would have been microscopic, cell-like organizations capable of replicating and adapting to environmental conditions -- a humble beginning to life on Earth.

"The current paradigm on the emergence of life is that RNA came first and in a high-temperature environment," Blaber said. "The data we are generating are much more in favor of a protein-first view in a halophile environment."

The widely accepted view among scientists is that RNA, found in all living cells, would have likely represented the first molecules of life, hypothesizing an "RNA-first" view of the origin of living systems from non-living molecules. Blaber's results indicate that the set of amino acids produced by simple chemical processes contains the requisite（必备的） information to produce complex folded proteins, which supports an opposing "protein-first" view.

Another prevailing view holds that a high-temperature (thermophile) environment, such as deep-ocean thermal vents, may have been the breeding ground for the origin of life. "The halophile, or salt-loving, environment has typically been considered one that life adapted into, not started in," Blaber said. "Our study of the prebiotic（生命起源以前的） amino acids and protein design and folding suggests the opposite."

Without the ability to fold, proteins would not be able to form the precise structures essential for functions that sustain life as we know it. Folding allows proteins to take on a globular shape through which they can interact with other proteins, perform specific chemical reactions, and adapt to enable organisms to exploit a given environment.

"There are numerous niches that life can evolve into," Blaber said. "For example, extremophiles are organisms that exist in high temperatures, high acidity, extreme cold, extreme pressure and extreme salt and so on. For life to exist in such environments it is essential that proteins are able to adapt in those conditions. In other words, they have to be able to fold."