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Structure solved by Scripps scientists shows one way that body controls gene expression

large repertoire of mechanisms for turning genes on and off. Many of the proteins encoded by genes in human and other genomes specialize in regulating other genes, often in complicated feedback mechanisms.

Shutting off the transcription of a gene -- the process whereby a single-stranded piece of messenger RNA (mRNA) is made from a double-stranded piece of DNA -- has for decades been recognized by molecular and cell biologists as a crucial way the cell regulates the expression of a gene.

In the last several years, many of these same scientists, including Wright and his colleagues, have been growing aware of the importance of post-transcriptional gene regulation, which occurs at the level of mRNA.

In mammals, once DNA genes are transcribed into mRNAs in the nucleus of a cell, they are usually transported outside the nucleus, where the mRNAs can be "translated" into proteins. At this point, certain regulatory proteins stabilize the mRNA, allowing it to be translated by the cell's machinery into proteins. Other regulatory proteins destabilize the mRNAs, marking them for degradation by the cell's machinery.

TIS11d belongs to a common family of regulatory proteins of this latter type. It regulates the levels of many important proteins involved in the body's inflammatory response, such as tumor necrosis factor (TNF) and interferons, by marking the TNF and interferon mRNAs for destruction. With incredible specificity, this protein uses its tandem zinc finger domain to recognize particular sequences of TNF and interferon mRNA.

By solving the structure, Wright and his colleagues revealed for the first time in atomic detail exactly how this recognition occurs.

The TIS11d protein basically mimics the base-pairing that takes place in DNA by using its tandem zinc finger domains to bind to the mRNA. Following the same principle that two strands of DNA use to bind to e
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Contact: Keith McKeown
kmckeown@scripps.edu
858-784-8134
Scripps Research Institute
13-Feb-2004


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