Low Thymine Content in PINK1 mRNAs and Insights into Parkinson's disease

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dc.contributor.author Anandagopu, P en_US
dc.contributor.author Rashid, S en_US
dc.contributor.author Li, Jinyan en_US
dc.contributor.editor en_US
dc.date.accessioned 2012-02-02T10:11:32Z
dc.date.available 2012-02-02T10:11:32Z
dc.date.issued 2010 en_US
dc.identifier 2011000542 en_US
dc.identifier.citation Anandagopu P, Rashid S, and Li Jinyan 2010, 'Low Thymine Content in PINK1 mRNAs and Insights into Parkinson's disease', Biomedical Informatics Publishing Group, vol. 4, no. 10, pp. 452-455. en_US
dc.identifier.issn 0973-2063 en_US
dc.identifier.other C1UNSUBMIT en_US
dc.identifier.uri http://hdl.handle.net/10453/15203
dc.description.abstract Thymine is the only nucleotide base which is changed to uracil upon transcription, leaving mRNA less hydrophobic compared to its DNA counterpart. All the 16 codons that contain uracil (or thymine in gene) as the second nucleotide code for the five large hydrophobic residues (LHRs), namely phenylalanine,v isoleucine, leucine, methionine and valine. Thymine content (i.e. the fraction of XTX codons, where X = A, C, G, or T) in PINK1 mRNA sequences and its relationship with protein stability and function are the focus of this work. This analysis will shed light on PINK1's stability, thus a clue can be provided to understand the mitochondrial dysfunction and the failure of oxidative stress control frequently observed in Parkinson's disease. We obtained the complete PINK1 mRNA sequences of 8 different species. The distributions of XTX codons in different frames are calculated. We observed that the thymine content reached the highest level in the coding frame 1 of the PINK1 mRNA sequence of Bos Taurus (Bt), that is peaked at 27%. Coding frame 1 containing low thymine leads to the reduction in LHRs in the corresponding proteins. Therefore, we conjecture that proteins from the other organisms, including Homo sapiens, lost some of their hydrophobicity and became susceptible to dysfunction. Genes such as PINK1 have reduced thymine in the evolutionary process thereby making their protein products potentially being susceptible to instability and causing disease. Adding more hydrophobic residues (thymine) at appropriate places might help conserve important biological functions. en_US
dc.language en_US
dc.publisher Biomedical Informatics Publishing Group en_US
dc.title Low Thymine Content in PINK1 mRNAs and Insights into Parkinson's disease en_US
dc.parent Bioinformation en_US
dc.journal.volume 4 en_US
dc.journal.number 10 en_US
dc.publocation India en_US
dc.identifier.startpage 452 en_US
dc.identifier.endpage 455 en_US
dc.cauo.name FEIT.Faculty of Engineering & Information Technology en_US
dc.conference Verified OK en_US
dc.for 089900 en_US
dc.personcode 0000072824 en_US
dc.personcode 0000072825 en_US
dc.personcode 112261 en_US
dc.percentage 100 en_US
dc.classification.name Other Information and Computing Sciences en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity en_US
dc.description.keywords thymine distribution, PINK1, sequence analysis, protein stability, frame analysis en_US
dc.staffid en_US
dc.staffid 112261 en_US


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