Tropomyosin: Difference between revisions

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=== Post-Translational Modifications ===

There are two types of post-translational modifications to tropomyosin: phosphorylation acetylation<ref name="Gunning"/>. Phosphorylation occurs on amino acid <scene name='User:Gregory_Hoeprich/Sandbox_1/Tropomyosin_dimer_ser229/1'>Ser-229</scene><ref name="Gunning"/>. This phosphorylation is occurs as a result of oxidative stress, which is associated with actin remodeling and recruitment of additional tropomyosin into stress fibers<ref name="Gunning"/>. The acetylation ~~occurs~~ occurs on the N-terminus of the N-terminal methionine, which is essential for: coiled-coil stability, overlap formation and actin binding<ref name="Frye"/><ref name="Gunning"/>.

There are two types of post-translational modifications to tropomyosin: phosphorylation acetylation<ref name="Gunning"/>. Phosphorylation occurs on amino acid <scene name='User:Gregory_Hoeprich/Sandbox_1/Tropomyosin_dimer_ser229/1'>Ser-229</scene><ref name="Gunning"/>. This phosphorylation is occurs as a result of oxidative stress, which is associated with actin remodeling and recruitment of additional tropomyosin into stress fibers<ref name="Gunning"/>. The acetylation occurs on the N-terminus of the N-terminal methionine, which is essential for: coiled-coil stability, overlap formation and actin binding<ref name="Frye"/><ref name="Gunning"/>.

=== Evolutionary Conservation ===

Tropomyosin is highly conserved actin binding protein, which is found in Eukarya from the animal kingdom to yeast, with the exception of plants<ref name="Gunning"/>. The earliest characterization of tropomyosin gene lineage was in yeast (budding and fission yeast)<ref name="Gunning"/><ref name="Drees">PMID:7844152</ref>. These genes are known as [http://en.wikipedia.org/wiki/TPM1 TPM1] and [http://en.wikipedia.org/wiki/TPM2 TPM2], respectively, and share 64.5% sequence identity<ref name="Gunning"/><ref name="Drees"/>. As we move away from unicellular organisms and into multicellular invertebrates, tropomyosin genes in nematodes slightly diverge from yeast, but have 85-90% sequence identity between their genes<ref name="Gunning"/>. Further analysis for vertebrates show there are four genes that generate over 40 known mammalian isoforms of tropomyosin, which are synthesized by exon splicing<ref name="Gunning"/>. The slight evolution change of tropomyosin has occurred as a result of the increasing need of tropomyosin to function in different systems, but tropomyosin has evolutionarily stayed well conserved because of the basic structural pressures imposed on the protein<ref name="Gunning"/>. It is interesting to note, the region with the least conservation has been in the N and C terminus. This is the result of head-tail interactions changing to accommodate different polymer confirmations along actin for different functions<ref name="Gunning"/>. (To see this evolutionary conservation, go to the top right image of the web page and click on the "show" link, which is to the right of "Evolutionary Conservation".)

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@@ Line 25: / Line 25: @@
 === Post-Translational Modifications ===
-There are two types of post-translational modifications to tropomyosin: phosphorylation acetylation<ref name="Gunning"/>.  Phosphorylation occurs on amino acid <scene name='User:Gregory_Hoeprich/Sandbox_1/Tropomyosin_dimer_ser229/1'>Ser-229</scene><ref name="Gunning"/>.  This phosphorylation is occurs as a result of oxidative stress, which is associated with actin remodeling and recruitment of additional tropomyosin into stress fibers<ref name="Gunning"/>.  The acetylation occurs occurs on the N-terminus  of the N-terminal methionine, which is essential for: coiled-coil stability, overlap formation and actin binding<ref name="Frye"/><ref name="Gunning"/>.
+There are two types of post-translational modifications to tropomyosin: phosphorylation acetylation<ref name="Gunning"/>.  Phosphorylation occurs on amino acid <scene name='User:Gregory_Hoeprich/Sandbox_1/Tropomyosin_dimer_ser229/1'>Ser-229</scene><ref name="Gunning"/>.  This phosphorylation is occurs as a result of oxidative stress, which is associated with actin remodeling and recruitment of additional tropomyosin into stress fibers<ref name="Gunning"/>.  The acetylation occurs on the N-terminus  of the N-terminal methionine, which is essential for: coiled-coil stability, overlap formation and actin binding<ref name="Frye"/><ref name="Gunning"/>.
 === Evolutionary Conservation ===
 Tropomyosin is highly conserved actin binding protein, which is found in Eukarya from the animal kingdom to yeast, with the exception of plants<ref name="Gunning"/>.  The earliest characterization of tropomyosin gene lineage was in yeast (budding and fission yeast)<ref name="Gunning"/><ref name="Drees">PMID:7844152</ref>.  These genes are known as [http://en.wikipedia.org/wiki/TPM1 TPM1] and [http://en.wikipedia.org/wiki/TPM2 TPM2], respectively, and share 64.5% sequence identity<ref name="Gunning"/><ref name="Drees"/>.  As we move away from unicellular organisms and into multicellular invertebrates, tropomyosin genes in nematodes slightly diverge from yeast, but have 85-90% sequence identity between their genes<ref name="Gunning"/>.  Further analysis for vertebrates show there are four genes that generate over 40 known mammalian isoforms of tropomyosin, which are synthesized by exon splicing<ref name="Gunning"/>.  The slight evolution change of tropomyosin has occurred as a result of the increasing need of tropomyosin to function in different systems, but tropomyosin has evolutionarily stayed well conserved because of the basic structural pressures imposed on the protein<ref name="Gunning"/>.  It is interesting to note, the region with the least conservation has been in the N and C terminus.  This is the result of head-tail interactions changing to accommodate different polymer confirmations along actin for different functions<ref name="Gunning"/>.  (To see this evolutionary conservation, go to the top right image of the web page and click on the "show" link, which is to the right of "Evolutionary Conservation".)