A
structural1 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
metabolic2 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
Proceedings3 of the National Academy of Sciences.
The first living organisms would have been
microscopic4, cell-like organizations capable of
replicating5 and adapting to environmental conditions -- a
humble6 beginning to life on Earth.
"The current
paradigm7 on the
emergence8 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
molecules9 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
requisite10(必备的) information to produce complex folded proteins, which supports an opposing "protein-first" view.
Another
prevailing11 view holds that a high-temperature (thermophile) environment, such as deep-ocean
thermal12 vents13, 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
niches14 that life can evolve into," Blaber said. "For example, extremophiles are organisms that exist in high temperatures, high
acidity15, 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."