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Scientists clarify structural basis for biosynthesis of mysterious 21st amino acid

Date:
August 14, 2010
Source:
RIKEN
Summary:
Researchers in Japan have clarified the structural basis for the biosynthesis of selenocysteine (Sec), an amino acid whose encoding mechanism offers clues about the origins of the genetic alphabet. The findings deepen our understanding of protein synthesis and lay the groundwork for advances in protein design.

Comparison of selenocysteine (Sec) to the structurally similar amino aids serine (Ser) and cysteine (Cys).
Credit: Image courtesy of RIKEN

Researchers at the RIKEN Systems and Structural Biology Center and the University of Tokyo have clarified the structural basis for the biosynthesis of selenocysteine (Sec), an amino acid whose encoding mechanism offers clues about the origins of the genetic alphabet. The findings deepen our understanding of protein synthesis and lay the groundwork for advances in protein design.

One of the most remarkable aspects of translation, the process whereby genetic information is converted into proteins in cells, is its universality: nucleotide triplets ("codons") encode a set of twenty amino acids that form the building blocks for all living organisms. Selenocysteine, the "21st amino acid" whose antioxidant properties help prevent cellular damage, is a rare exception to this rule. Structurally similar to the amino acid serine (Ser) but with an oxygen atom replaced by the micronutrient selenium (Se), selenocysteine is synthesized through a complex juggling of the cell's translational machinery whose mechanisms remain poorly understood.

Central to this multi-step process is a Sec-specific transfer RNA (tRNASec) with an unusual structure that enables it to hijack the "stop codon" UGA to allow incorporation of selenocysteine during protein synthesis. In earlier work, the researchers identified features of tRNASec that differentiate it from other tRNA, notably the peculiar structure of a domain called the D-arm, which appeared to act as an identification marker for recognition by the selenocysteine synthesis machinery. This time, the team analyzed the D-arm's role in the interaction of tRNASec with O-phosphoseryl-tRNA kinase (PSTK), a protein whose selective phosphorylation is essential for selenocysteine encoding.

Using X-ray crystallography, the team showed for the first time that it is the unique structure of the tRNASec D-arm which enables PSTK to distinguish tRNASec from other tRNA. Reported in the August 13 issue of Molecular Cell (online August 12), the discovery clarifies a pivotal step in selenocysteine biosynthesis, shedding new light on the mysterious 21st amino acid and the elaborate process by which it is created.


Story Source:

The above story is based on materials provided by RIKEN. Note: Materials may be edited for content and length.


Journal Reference:

  1. Shiho Chiba, Yuzuru Itoh, Shun-ichi Sekine and Shigeyuki Yokoyama. Structural Basis for the Major Role of O-Phosphoseryl-tRNA Kinase in the UGA-Specific Encoding of Selenocysteine. Molecular Cell, 2010; 39: 1-11 DOI: 10.1016/j.molcel.2010.07.018

Cite This Page:

RIKEN. "Scientists clarify structural basis for biosynthesis of mysterious 21st amino acid." ScienceDaily. ScienceDaily, 14 August 2010. <www.sciencedaily.com/releases/2010/08/100812171939.htm>.
RIKEN. (2010, August 14). Scientists clarify structural basis for biosynthesis of mysterious 21st amino acid. ScienceDaily. Retrieved July 26, 2014 from www.sciencedaily.com/releases/2010/08/100812171939.htm
RIKEN. "Scientists clarify structural basis for biosynthesis of mysterious 21st amino acid." ScienceDaily. www.sciencedaily.com/releases/2010/08/100812171939.htm (accessed July 26, 2014).

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