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RLL comments edit

Overall I like this. Good work.

 
The collagen triple helix is a triple helix formed from three separate protein helices, spiraling around the same axis.

Hey, what's up. I'm drafting improvements to the Triple Helix page. If you have any input to the stuff I have going, let me know on my talk page or something.

In geometry, a triple helix (plural triple helices) is a set of three congruent geometrical helices with the same axis, differing by a translation along the axis. This means that each of the helices keeps the same distance from the central axis. As with a single helix, a triple helix may be characterized by its pitch and diameter. Examples of triple helices include triplex DNA[1], RNA[2], collagen[3] and collagen-like proteins.

General Structure edit

A triple helix is named such because it is made up of three separate helices. Each of these helices shares the same axis, but they do not take up the same space because each helix is translated angularly around the axis. Generally, the identity of a triple helix depends on the type of helices that make it up. For example: a triple helix made of three strands of collagen protein is a collagen triple helix, and a triple helix made of three strands of DNA is a DNA triple helix.

As with other types of helices, triple helices have handedness: right-handed or left-handed. A right-handed helix moves around its axis in a clockwise direction from beginning to end. A left-handed helix is the right-handed helix's mirror image, and it moves around the axis in a counterclockwise direction from beginning to end.[4] The beginning and end of a helical molecule are defined based on certain markers in the molecule that do not change easily. For example: the beginning of a helical protein is its N terminus, and the beginning of a single strand of DNA is its 5' end.[4]

Peer Review AJL: It would be nice to have a citation for this general stuff in the preceding two paragraphs.

The collagen triple helix is made of three collagen peptides, each of which forms its own left-handed polyproline helix.[5] When the three chains combine, the triple helix adopts a right-handed orientation. The collagen peptide is composed of repeats of Gly-X-Y, with the second residue (X) usually being Pro and the third (Y) being hydroxyproline.[6][5]

A DNA triple helix is made up of three separate DNA strands, each oriented with the sugar/phosphate backbone on the outside of the helix and the bases on the inside of the helix. The bases are the part of the molecule closest to the triple helix's axis, and the backbone is the part of the molecule farthest away from the axis. The third strand occupies the major groove of relatively normal duplex DNA.[7] The bases in triplex DNA are arranged to match up according to a Hoogsteen base pairing scheme.[8] Similarly, RNA triple helices are formed as a result of a single stranded RNA forming hydrogen bonds with an RNA duplex; the duplex consists of Watson-Crick base pairing while the third strand binds via Hoogsteen base pairing.[9]

Stabilizing Factors edit

The collagen triple helix has several characteristics that increase its stability. When proline is incorporated into the Y position of the Gly-X-Y sequence, it is post-translationally modified to hydroxyproline.[10] The hydroxyproline can enter into favorable interactions with water, which stabilizes the triple helix because the Y residues are solvent-accessible in the triple helix structure. The individual helices are also held together by an extensive network of amide-amide hydrogen bonds formed between the strands, each of which contributes approximately -2 kcal/mol to the overall free energy of the triple helix.[5] The formation of the superhelix protects the critical glycine residues on the interior of the helix in addition to protecting the overall protein from proteolysis.[6]

Peer Review AJL: Maybe change the wording of the last sentence to make more sense. Perhaps "The formation of the superhelix not only protects the critical glycine residues on the interior of the helix, but also protects the overall protein from proteolysis."

Triple helix DNA and RNA are stabilized by many of the same forces that stabilize double-stranded DNA helices. With nucleotide bases oriented to the inside of the helix, closer to its axis, bases engage in hydrogen bonding with other bases. The bonded bases in the center exclude water, so the hydrophobic effect is particularly important in the stabilization of DNA triple helices.[4]

PR AJL: You should include a source here that talks about the hydrophobic effect or hydrogen bonding stabilizing either double or triple helices.

Biological Role edit

Proteins edit

Members of the collagen superfamily are major contributors to the extracellular matrix. The triple helical structure provides strength and stability to collagen fibers by providing great resistance to tensile stress. The rigidity of the collagen fibers is an important factor that can withstand most mechanical stress, making it an ideal protein for macromolecular transport and overall structural support throughout the body.[6]

DNA edit

There are some oligonucleotide sequences, called triplet-forming oligonucleotides (TFOs) that can bind to form a triplex with a longer molecule of double-stranded DNA; TFOs can inactivate a gene or help to induce mutations.[7] TFOs can only bind to certain sites in a larger molecule, so researchers must first determine whether a TFO can bind to the gene of interest.

RNA edit

In recent years, the biological function of triplex RNA has become more studied. Some roles include increasing stability, translation, influencing ligand binding, and catalysis. One example of ligand binding being influenced by a triple helix is in the SAM-II riboswitch where the triple helix creates a binding site that will uniquely accept S-adenosylmethionine (SAM).[9] The ribonucleoprotein complex telomerase, responsible for replicating the tail-ends of DNA (telomeres) also contains triplex RNA believed to be necessary for proper telomerase functioning.[9][11] The triple helix at the 3' end of MALAT1 serves to stabilize the RNA by protecting the Poly-A tail from proteolysis as well as increases translation efficiency, which is ultimately detrimental to humans as MALAT1 is related to lung cancer malignancy.[9][12]

References edit

  1. ^ Bernués, J.; Azorín, F. (1995), "Triple-Stranded DNA", Nucleic Acids and Molecular Biology, Springer Berlin Heidelberg, pp. 1–21, doi:10.1007/978-3-642-79488-9_1, ISBN 9783642794902, retrieved 2018-10-10
  2. ^ Buske, Fabian A.; Mattick, John S.; Bailey, Timothy L. (2011-05). "Potential in vivo roles of nucleic acid triple-helices". RNA Biology. 8 (3): 427–439. doi:10.4161/rna.8.3.14999. ISSN 1547-6286. PMC 3218511. PMID 21525785. {{cite journal}}: Check date values in: |date= (help)CS1 maint: PMC format (link)
  3. ^ Bächinger, Hans Peter (2005-05-03). Collagen: Primer in Structure, Processing and Assembly. Springer Science & Business Media. ISBN 9783540232728.
  4. ^ a b c John,, Kuriyan,. The molecules of life : physical and chemical principles. Konforti, Boyana,, Wemmer, David,. New York. ISBN 9780815341888. OCLC 779577263.{{cite book}}: CS1 maint: extra punctuation (link) CS1 maint: multiple names: authors list (link)
  5. ^ a b c Shoulders, Matthew D.; Raines, Ronald T. (2009). "COLLAGEN STRUCTURE AND STABILITY". Annual review of biochemistry. 78: 929–958. doi:10.1146/annurev.biochem.77.032207.120833. ISSN 0066-4154. PMC 2846778. PMID 19344236.{{cite journal}}: CS1 maint: PMC format (link)
  6. ^ a b c Fidler, Aaron L.; Boudko, Sergei P.; Rokas, Antonis; Hudson, Billy G. (2018-04-01). "The triple helix of collagens – an ancient protein structure that enabled animal multicellularity and tissue evolution". J Cell Sci. 131 (7): jcs203950. doi:10.1242/jcs.203950. ISSN 0021-9533. PMC 5963836. PMID 29632050.{{cite journal}}: CS1 maint: PMC format (link)
  7. ^ a b Jain, Aklank; Wang, Guliang; Vasquez, Karen M. (2008-8). "DNA Triple Helices: biological consequences and therapeutic potential". Biochimie. 90 (8): 1117–1130. doi:10.1016/j.biochi.2008.02.011. ISSN 0300-9084. PMC 2586808. PMID 18331847. {{cite journal}}: Check date values in: |date= (help)CS1 maint: PMC format (link)
  8. ^ Duca, Maria; Vekhoff, Pierre; Oussedik, Kahina; Halby, Ludovic; Arimondo, Paola B. (2008-9). "The triple helix: 50 years later, the outcome". Nucleic Acids Research. 36 (16): 5123–5138. doi:10.1093/nar/gkn493. ISSN 0305-1048. PMC 2532714. PMID 18676453. {{cite journal}}: Check date values in: |date= (help)CS1 maint: PMC format (link)
  9. ^ a b c d Conrad, Nicholas K. (2014). "The emerging role of triple helices in RNA biology". Wiley interdisciplinary reviews. RNA. 5 (1): 15–29. doi:10.1002/wrna.1194. ISSN 1757-7004. PMC 4721660. PMID 24115594.{{cite journal}}: CS1 maint: PMC format (link)
  10. ^ Brodsky, B; Persikov, AV (2005-01-01). "Molecular Structure of the Collagen Triple Helix". Advances in Protein Chemistry. 70: 301–339. doi:10.1016/S0065-3233(05)70009-7. ISSN 0065-3233.
  11. ^ Theimer, Carla A.; Blois, Craig A.; Feigon, Juli (2005-03-04). "Structure of the human telomerase RNA pseudoknot reveals conserved tertiary interactions essential for function". Molecular Cell. 17 (5): 671–682. doi:10.1016/j.molcel.2005.01.017. ISSN 1097-2765. PMID 15749017.
  12. ^ Brown, Jessica A.; Bulkley, David; Wang, Jimin; Valenstein, Max L.; Yario, Therese A.; Steitz, Thomas A.; Steitz, Joan A. (2014-7). "Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix". Nature Structural & Molecular Biology. 21 (7): 633–640. doi:10.1038/nsmb.2844. ISSN 1545-9985. PMC 4096706. PMID 24952594. {{cite journal}}: Check date values in: |date= (help)CS1 maint: PMC format (link)
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