New Measurement for Correlation of Co-evolution Relationship of Subsequences in Protein
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  • 作者:Hongyun Gao ; Xiaoqing Yu ; Yongchao Dou…
  • 关键词:Mutual information ; Adjacent ; Correlation ; Subsequence ; Pearson’s correlation coefficient
  • 刊名:Interdisciplinary Sciences: Computational Life Sciences
  • 出版年:2015
  • 出版时间:December 2015
  • 年:2015
  • 卷:7
  • 期:4
  • 页码:364-372
  • 全文大小:721 KB
  • 参考文献:1.Ambrogelly A, Palioura S, S?ll D (2007) Natural expansion of the genetic code. Nat Chem Biol 3(1):29-5CrossRef PubMed
    2.Bystroff C, Shao Y (2002) Fully automated ab initio protein structure prediction using i-sites, hmmstr and rosetta. Bioinformatics 18(suppl 1):S54–S61CrossRef PubMed
    3.Eddy SR (1998) Profile hidden markov models. Bioinformatics 14(9):755-63CrossRef PubMed
    4.Nimrod G, Glaser F, Steinberg D, Ben-Tal N, Pupko T (2005) In silico identification of functional regions in proteins. Bioinformatics 21:i328-7CrossRef PubMed
    5.Jukes T, Cantor C (1969) Evolution of protein molecules. In: Munro H (ed) Mammalian protein metabolism. Academic Press, New York, USA, pp 21-32CrossRef
    6.Atchley WR, Wollenberg KR, Fitch WM, Terhalle W, Dress AW (2000) Correlations among amino acid sites in bhlh protein domains: an information theoretic analysis. Mol Biol Evol 17(1):164-78CrossRef PubMed
    7.Barabási AL, Oltvai ZN (2004) Network biology: understanding the cell’s functional organization. Nat Rev Genet 5:101-13CrossRef PubMed
    8.Goh CS, Bogan AA, Joachimiak M, Walther D, Cohen FE (2000) Co-evolution of proteins with their interaction partners. J Mol Biol 299(2):283-93CrossRef PubMed
    9.Pazos F, Helmer-Citterich M, Ausiello G, Valencia A (1997) Correlated mutations contain information about protein–protein interaction. J Mol Biol 271(4):511-23CrossRef PubMed
    10.Fraser HB, Hirsh AE, Wall DP, Eisen MB (2004) Coevolution of gene expression among interacting proteins. PNAS 101(24):9033-038PubMed Central CrossRef PubMed
    11.Pazos F, Valencia A (2001) Similarity of phylogenetic tree as indicator of protein–protein interaction. Protein Eng 14(9):609-14CrossRef PubMed
    12.Atwell S, Ultsch M, Vos AMD, Wells JA (1997) Structural plasticity in a remodeled protein-protein interface. Science 278(5340):1125-128CrossRef PubMed
    13.Chelvanayagam G, Eggenschwiler A, Knecht L, Gonnet G, Benner S (1997) An analysis of simultaneous variation in protein structures. Protein Eng 10:307-16CrossRef PubMed
    14.Goh CS, Cohen FE (2002) Coevolutionary analysis reveals insights into protein–protein interactions. J Mol Biol 324(1):177-92CrossRef PubMed
    15.Martin LC, Gloor GB, Dunn SD, Wahl LM (2005) Using information theory to search for co-evolving residues in proteins. Bioinformatics 21(22):4116-124CrossRef PubMed
    16.Olivera L, Paiva ACM, Vriend G (2002) Correlated mutation analyses on very large sequence families. Chem Bio Chem 3(10):1010-017CrossRef
    17.Taylor WR, Hatrick K (1994) Compensating changes in protein multiple sequence alignments. Protein Eng 7(3):341-48CrossRef PubMed
    18.Chakrabarti S, Panchenko A (2009) Coevolution in defining the functional specificity. Proteins 75(1):231-40PubMed Central CrossRef PubMed
    19.Dimmic MW, Hubisz MJ, Bustamante CD, Nielsen R (2005) Detecting coevolving amino acid sites using Bayesian mutational mapping. Bioinformatics 21(suppl 1):126-35CrossRef
    20.Fares MA (2006) Computational and statistical methods to explore the various dimensions of protein evolution. Curr Bioinform 1:207-17CrossRef
    21.Fares MA, McNally D (2006) Caps: coevolution analysis using protein sequences. Bioinformatics 22(22):2821-822CrossRef PubMed
    22.Fasold M, Stadler PF, Binder H (2010) G-stack modulated probe intensities on expression arrays-sequence corrections and signal calibration. BMC Bioinform 11:207CrossRef
    23.Gao H, Dou Y, Yang J, Wang J (2011) New methods to measure residues coevolution in proteins. BMC Bioinform 12:206CrossRef
    24.Gloor GB, Martin LC, Wahl LM, Dunn SD (2005) Mutual information in protein multiple sequence alignments reveals two classes of coevolving positions. Biochemistry 44(19):7156-165CrossRef PubMed
    25.Pollock DD, Taylor WR, Goldman N (1999) Coevolving protein residues: maximum likelihood identification and relationship to structure. J Mol Biol 287(1):187-98CrossRef PubMed
    26.Weckwerth W, Selbig J (2003) Scoring and identifying organism-specific functional patterns and putative phosphorylation sites in protein sequences using mutual information. Biochem Biophys Res Commun 307:516-21CrossRef PubMed
    27.Hassan SS, Choudhury PP, Guha R, Chakraborty S, Goswami A (2012) Dna sequence evolution through integral value transformations. Interdiscip Sci 4:128-32CrossRef PubMed
    28.Silviu G (1977) Information theory with applications. McGraw-Hill, New York
    29.Halabi N, Rivoire O, Leibler S, Ranganathan R (2009) Protein sectors: evolutionary units of three-dimensional structure. Cell 138:774-86PubMed Central CrossRef PubMed
    30.McLaughlin RN Jr, Poelwijk FJ, Raman A, Gosal WS, Ranganathan R (2012) The spatial architecture of protein function and adaptation. Nature 491:138-42PubMed Central CrossRef PubMed
    31.Lockless SW, Ranganathan R (1999) Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286(5438):295-99CrossRef PubMed
    32.Russ WP, Lowery
  • 作者单位:Hongyun Gao (1) (2)
    Xiaoqing Yu (3)
    Yongchao Dou (4)
    Jun Wang (5)

    1. School of Mathematical Sciences, Dalian University of Technology, Dalian, 116024, China
    2. Information and Engineering College, Dalian University, Dalian, 116622, China
    3. College of Sciences, Shanghai Institute of Technology, Shanghai, 201418, China
    4. Center for Plant Science and Innovation, School of Biological Sciences, University of Nebraska, Lincoln, NE, 68588, USA
    5. Department of Mathematics, Shanghai Normal University, Shanghai, 200234, China
  • 刊物主题:Computer Appl. in Life Sciences; Computational Biology/Bioinformatics; Statistics for Life Sciences, Medicine, Health Sciences; Theoretical and Computational Chemistry; Theoretical, Mathematical and Computational Physics; Computational Science and Engineering;
  • 出版者:International Association of Scientists in the Interdisciplinary Areas
  • ISSN:1867-1462
文摘
Many computational tools have been developed to measure the protein residues co-evolution. Most of them only focus on co-evolution for pairwise residues in a protein sequence. However, number of residues participate in co-evolution might be multiple. And some co-evolved residues are clustered in several distinct regions in primary structure. Therefore, the co-evolution among the adjacent residues and the correlation between the distinct regions offer insights into function and evolution of the protein and residues. Subsequence is used to represent the adjacent multiple residues in one distinct region. In the paper, co-evolution relationship in each subsequence is represented by mutual information matrix (MIM). Then, Pearson’s correlation coefficient: R value is developed to measure the similarity correlation of two MIMs. MSAs from Catalytic Data Base (Catalytic Site Atlas, CSA) are used for testing. R value characterizes a specific class of residues. In contrast to individual pairwise co-evolved residues, adjacent residues without high individual MI values are found since the co-evolved relationship among them is similar to that among another set of adjacent residues. These subsequences possess some flexibility in the composition of side chains, such as the catalyzed environment. Keywords Mutual information Adjacent Correlation Subsequence Pearson’s correlation coefficient

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