Homology between DUF784, DUF1278 domains and the plant prolamin superfamily typifies evolutionary changes of disulfide bonding patterns

Cell Cycle

Volumn 8, Issue 20, 2009, Pages 3428-3430

  Zhang, Dapeng ^a  

^a UNIVERSITY OF OTTAWA   (Canada)

Author keywords

Disulfide bond; DUF1278; DUF784; Evolution; Fold recognition; Plant allergen; Prolamin superfamily

Indexed keywords

CYSTEINE; PROLAMIN;

ALPHA HELIX; ARABIDOPSIS; BETA SHEET; CONTROLLED STUDY; DISULFIDE BOND; EVOLUTIONARY HOMOLOGY; LETTER; NONHUMAN; PLANT GENOME; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS;

EID: 70350212953     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.8.20.9674     Document Type: Letter

References (17)

1. Shewry PR, Beaudoin F, Jenkins J, Griffiths-Jones S, Mills EN. Plant protein families and their relationships to food allergy. Biochem Soc Trans 2002; 30:906-910 (Pubitemid 36002377)
2. Breiteneder H, Mills EN. Molecular properties of food allergens. J Allergy Clin Immunol 2005; 115:14-23.
3. Finn RD, Tate J, Mistry J, Coggill PC, Sammut SJ, Hotz HR, et al. The Pfam protein families database. Nucleic Acids Res 2008; 36:281-288
4. Egorov TA, Odintsova TI, Musolyamov AKh, Fido R, Tatham AS, Shewry PR. Disulphide structure of a sunflower seed albumin: conserved and variant disulphide bonds in the cereal prolamin superfamily. FEBS Letters 1996; 396:285-288 (Pubitemid 26377841)
5. Oda Y, Matsunaga T, Fukuyama K, Miyazaki T, Morimoto T. Tertiary and quaternary structures of 0.19 alpha-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 A resolution. Biochemistry 1997; 36:13503-13511 (Pubitemid 27481596)
6. Jones-Rhoades M, et al. Plos Genet 2007; 3:171.
7. Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W, et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997; 25:3389-3402 (Pubitemid 27359211)
8. Shi J, Blundell TL, Mizuguchi K. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 2001; 310:243-257 (Pubitemid 32619966)
9. Jaroszewski L, Rychlewski L, Li Z, Li W, Godzik A. FFAS03: a server for profile-profile sequence alignments. Nucleic Acids Res 2005; 33:284-288 (Pubitemid 44529927)
10. Zhang D, Trudeau VL. The XS domain of a plant specific SGS3 protein adopts a unique RNA recognition motif (RRM) fold. Cell Cycle 2008; 7:2268-2270 (Pubitemid 352031529)
11. Zhang D, Xiong H, Shan J, Xia X, Trudeau VL. Functional insight into Maelstrom in the germline piRNA pathway: a unique domain homologous to the DnaQ-H 3'-5' exonuclease, its lineage-specific expansion/ loss and evolutionarily active site switch. Biol Direct 2008; 3:48.
12. Edgar R. MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 2004; 5:113. (Pubitemid 40195393)
13. Pei J, Kim BH, Tang M, Grishin NV. PROMALS web server for accurate multiple protein sequence alignments. Nucleic Acids Res 2007; 35:649-652
14. Thornton J. Disulphide bridges in globular proteins. J Mol Biol 1981; 151:261-287
15. Herman W, et al. J Mol Biol 2004; 335:1083-1092
16. van Vlijmen HW, Gupta A, Narasimhan LS, Singh J. A novel database of disulfide patterns and its application to the discovery of distantly related homologs. Protein Sci 2004; 13:2045-2058
17. Thangudu RR, Sharma P, Srinivasan N, Offmann B. Analycys: a database for conservation and conformation of disulphide bonds in homologous protein domains. Proteins 2007; 67:255-261 (Pubitemid 46453738)