User:Katie Huff/Smaug Protein.
From Proteopedia
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==Smaug Protein== | ==Smaug Protein== | ||
<StructureSection load='1OXJ' size='350' side='right' caption='Smaug Protein (PDB entry [[1OXJ]])' size='350' frame='true' align='right' caption='Insert caption here' /> | <StructureSection load='1OXJ' size='350' side='right' caption='Smaug Protein (PDB entry [[1OXJ]])' size='350' frame='true' align='right' caption='Insert caption here' /> | ||
| - | '''Smaug protein''' is involved with RNA-binding and translation inhibition. Specifically, Smaug is involved in anterior-posterior segmentation of the embryo during [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] embryonic development. Smaug also plays a role in the [http://en.wikipedia.org/wiki/Midblastula midblastula transition] of ''D. melanogaster'' development. [[ | + | '''Smaug protein''' is involved with RNA-binding and translation inhibition. Specifically, Smaug is involved in anterior-posterior segmentation of the embryo during [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] embryonic development. Smaug also plays a role in the [http://en.wikipedia.org/wiki/Midblastula midblastula transition] of ''D. melanogaster'' development. [[2]] |
==Function== | ==Function== | ||
Most eukaryotes rely on maternal mRNA in early development because they synthesize the proteins that control the primary events of [http://en.wikipedia.org/wiki/Drosophila_embryogenesis embryogenesis] (cell fate decisions, axis determination, etc.). Because maternal mRNAs are already present at the time of fertilization, their subsequent expression must be restricted post-transcriptionally [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3078745/]. | Most eukaryotes rely on maternal mRNA in early development because they synthesize the proteins that control the primary events of [http://en.wikipedia.org/wiki/Drosophila_embryogenesis embryogenesis] (cell fate decisions, axis determination, etc.). Because maternal mRNAs are already present at the time of fertilization, their subsequent expression must be restricted post-transcriptionally [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3078745/]. | ||
| - | Smaug protein functions to regulate the posterior pole of the embryo by inhibiting translation of maternal ''nanos'' mRNA. Smaug effectively performs this task by binding to the 3'UTR region of the ''nanos'' mRNA. This prevents ''nanos'' from passively diffusing to the posterior cortex of the embryo and undergoing translation. Smaug protein's mechanism of action involves the recruitment of another protein called CUP up binding to the 3'UTR region of ''nanos'' mRNA. Together, they prevent the association with a ribosome that would trigger translation. The ''nanos''-Smaug-CUP complex can be undone, however, if the complex reaches the posterior cortex. In this case, the complex will be disassembled, which allows the mRNA to prepare it's message for translation [[ | + | Smaug protein functions to regulate the posterior pole of the embryo by inhibiting translation of maternal ''nanos'' mRNA. Smaug effectively performs this task by binding to the 3'UTR region of the ''nanos'' mRNA. This prevents ''nanos'' from passively diffusing to the posterior cortex of the embryo and undergoing translation. Smaug protein's mechanism of action involves the recruitment of another protein called CUP up binding to the 3'UTR region of ''nanos'' mRNA. Together, they prevent the association with a ribosome that would trigger translation. The ''nanos''-Smaug-CUP complex can be undone, however, if the complex reaches the posterior cortex. In this case, the complex will be disassembled, which allows the mRNA to prepare it's message for translation [[2]] |
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==Text References == | ==Text References == | ||
<references/> | <references/> | ||
| - | [[1]] Gilbert, Scott F. Developmental Biology. 9th ed. Sunderland, MA: Sinauer Associates, 2006. p. 206;222. | + | [[1]] Andrews, S. et. al. (2011). "Multiple Mechanisms Collaborate to Repress Nanos Translation in the Drosophila Ovary and Embryo." ''RNA Society'' 17.5 (2011): 967-77. |
| + | [[2]] Gilbert, Scott F. ''Developmental Biology''. 9th ed. Sunderland, MA: Sinauer Associates, 2006. p. 206;222. | ||
Revision as of 17:56, 16 April 2014
Contents |
Smaug Protein
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Smaug protein is involved with RNA-binding and translation inhibition. Specifically, Smaug is involved in anterior-posterior segmentation of the embryo during Drosophila melanogaster embryonic development. Smaug also plays a role in the midblastula transition of D. melanogaster development. 2
Function
Most eukaryotes rely on maternal mRNA in early development because they synthesize the proteins that control the primary events of embryogenesis (cell fate decisions, axis determination, etc.). Because maternal mRNAs are already present at the time of fertilization, their subsequent expression must be restricted post-transcriptionally [1]. Smaug protein functions to regulate the posterior pole of the embryo by inhibiting translation of maternal nanos mRNA. Smaug effectively performs this task by binding to the 3'UTR region of the nanos mRNA. This prevents nanos from passively diffusing to the posterior cortex of the embryo and undergoing translation. Smaug protein's mechanism of action involves the recruitment of another protein called CUP up binding to the 3'UTR region of nanos mRNA. Together, they prevent the association with a ribosome that would trigger translation. The nanos-Smaug-CUP complex can be undone, however, if the complex reaches the posterior cortex. In this case, the complex will be disassembled, which allows the mRNA to prepare it's message for translation 2 .
Disease
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
About this Structure
1oxj is a 1 chain structure with sequence from D. melanogaster. Full crystallographic information is available from OCA.
Structure Reference
- Green JB, Gardner CD, Wharton RP, Aggarwal AK. RNA recognition via the SAM domain of Smaug. Mol Cell. 2003 Jun;11(6):1537-48. PMID:12820967
Text References
1 Andrews, S. et. al. (2011). "Multiple Mechanisms Collaborate to Repress Nanos Translation in the Drosophila Ovary and Embryo." RNA Society 17.5 (2011): 967-77. 2 Gilbert, Scott F. Developmental Biology. 9th ed. Sunderland, MA: Sinauer Associates, 2006. p. 206;222.
