Genome complexity: ribosomes make proteins (Introduction)

by David Turell , Friday, February 03, 2017, 02:03 (2640 days ago) @ David Turell

It is turning out to be a highly complex organic chemical process:

https://phys.org/news/2017-02-protein-chaperone-job.html

"For proteins, this would be the equivalent of the red-carpet treatment: each protein belonging to the complex machinery of ribosomes—components of the cell that produce proteins—has its own chaperone to guide it to the right place at the right time and protect it from harm.

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"In all cells, genetic information is stored as DNA and transcribed into mRNAs that code for proteins. Ribosomes translate the mRNAs into amino acids, linking them together into polypeptide chains that fold into proteins. More than a million ribosomes are produced per day in an animal cell.

"Building ribosomes is a formidable undertaking for the cell, involving about 80 proteins that make up the ribosome itself, strings of ribosomal RNA, and more than 200 additional proteins that guide and regulate the process. "Ribosome assembly is a dynamic process, where everything happens in a certain order. We are only now beginning to elucidate the many steps involved," says Hoelz.

"To make matters more complex, the proteins making up a ribosome are first synthesized outside the nucleus of a cell, in the cytoplasm, before being transported into the nucleus where the initial stages of ribosome assembly take place.

"Chaperone proteins help transport ribosomal proteins to the nucleus while also protecting them from being chopped up by a cell's protein shredding machinery. The components that specifically aim this machinery at unprotected ribosomal proteins, ....ensures that equal numbers of the various ribosomal proteins are available for building the massive structure of a ribosome.

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"...a ribosomal protein called L4 is bound by a chaperone called "Assembly chaperone of RpL4," or Acl4. The chaperone ushers L4 through the nucleus, protecting it from harm, and delivers it to a developing ribosome at a precise time and location.

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"Hoelz says that the structure was a surprise because it was not known previously that chaperones hold on to their ribosomal proteins so tightly. He says they want to study other chaperones in the future to see if they function in a similar fashion to tightly guard ribosomal proteins."

Comment: In living biochemistry the actions of the genome are demonstrably extremely complex, defying simple chance creation. Saltation by a brilliant mind is the only answer to the origin that seems correct.