Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Minireview cung cấp cho các bạn kiến thức về ngành y đề tài: Regulating highly dynamic unstructured proteins and their coding mRNAs. | Minireview Regulating highly dynamic unstructured proteins and their coding mRNAs Buyong Ma and Ruth Nussinov Addresses Basic Research Program SAIC-Frederick Inc Center for Cancer Research Nanobiology Program NCI-Frederick Frederick MD 21702 USA. fSackler Institute of Molecular Medicine Department of Human Genetics and Molecular Medicine Sackler School of Medicine Tel Aviv University Tel Aviv 69978 Israel. Correspondence Ruth Nussinov. Email ruthnu@ Published 28 January 2009 Genome Biology 2009 10 204 doi gb-2009-10-1-204 The electronic version of this article is the complete one and can be found online at http 2009 10 1 204 2009 BioMed Central Ltd Abstract The lifetimes and conformations of intrinsically unstructured proteins IUPs and their mRNAs are orchestrated to ensure precision speed and flexibility in biological control. The complexity of a protein sequence - that is its information content - is related to structure and function 1 2 . As far as we know sequences of proteins with defined structures tend to have higher sequence complexity whereas sequences of intrinsically unstructured proteins IUPs are of lower complexity. A significant part of an IUP is devoid of a stable three-dimensional structure when free unbound in solution. Unstructured or disordered proteins are known to have numerous vital functions 2 and simple sequences apparently evolve more rapidly than those of highly structured proteins 3 . Living systems have either adapted to IUPs very early in evolution or have evolved complex mechanisms to take advantage of their properties at a later stage. A recent report in Science by Gsponer et al. 4 indicates that in yeast regardless of evolutionary time scale the regulation of the production maintenance and function of unstructured proteins can occur at multiple levels during mRNA transcription and degradation during protein translation and degradation and by controlling the fidelity of transcription and .
