메뉴 건너뛰기




Volumn 6, Issue , 2005, Pages

Chicken genome analysis reveals novel genes encoding biotin-binding proteins related to avidin family

Author keywords

[No Author keywords available]

Indexed keywords

AVIDIN; BINDING PROTEIN; BIOTIN; COMPLEMENTARY DNA;

EID: 25444490147     PISSN: 14712164     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/1471-2164-6-41     Document Type: Article
Times cited : (15)

References (58)
  • 3
    • 0023151126 scopus 로고
    • Role of avidin and other biotinbinding proteins in the deposition and distribution of biotin in chicken eggs. Discovery of a new biotin-binding protein
    • White HB III, Whitehead CC: Role of avidin and other biotinbinding proteins in the deposition and distribution of biotin in chicken eggs. Discovery of a new biotin-binding protein. Biochem J 1987, 241:677-684.
    • (1987) Biochem. J. , vol.241 , pp. 677-684
    • White III, H.B.1    Whitehead, C.C.2
  • 4
    • 0024598555 scopus 로고
    • Conversion of domains into subunits in the processing of egg yolk biotin-binding protein I
    • Bush L, White HB III: Conversion of domains into subunits in the processing of egg yolk biotin-binding protein I. J Biol Chem 1989, 264:5741-5745.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5741-5745
    • Bush, L.1    White III, H.B.2
  • 5
    • 0021892962 scopus 로고
    • Biotin-binding proteins and biotin transport to oocytes
    • White HB III: Biotin-binding proteins and biotin transport to oocytes. Ann N Y Acad Sci 1985, 447:202-11.
    • (1985) Ann. N. Y. Acad. Sci. , vol.447 , pp. 202-211
    • White III, H.B.1
  • 6
    • 0023647650 scopus 로고
    • Identification and molecular characterisation of a biotin-binding protein distinct from avidin of chicken egg white and comparison with yolk biotin-binding protein
    • Seshagiri PB, Adiga PR: Identification and molecular characterisation of a biotin-binding protein distinct from avidin of chicken egg white and comparison with yolk biotin-binding protein. Biochim Biophys Acta 1987, 926:321-30.
    • (1987) Biochim. Biophys. Acta , vol.926 , pp. 321-330
    • Seshagiri, P.B.1    Adiga, P.R.2
  • 7
    • 0018083932 scopus 로고
    • Biotin-binding protein from egg yolk. A protein distinct from egg white avidin
    • Meslar HW, Camper SA, White HB III: Biotin-binding protein from egg yolk. A protein distinct from egg white avidin. J Biol Chem 1978, 253:6979-6982.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6979-6982
    • Meslar, H.W.1    Camper, S.A.2    White III, H.B.3
  • 8
    • 0033621280 scopus 로고    scopus 로고
    • Foreword and introduction to the book (strept)avidin biotin system
    • Wilchek M, Bayer EA: Foreword and introduction to the book (strept)avidin biotin system. Biomol Eng 1999, 16:1-4.
    • (1999) Biomol. Eng. , vol.16 , pp. 1-4
    • Wilchek, M.1    Bayer, E.A.2
  • 9
    • 0029061527 scopus 로고
    • Simultaneous purification of biotinbinding proteins-I and -II from chicken egg yolk and their characterization
    • Subramanian N, Adiga PR: Simultaneous purification of biotinbinding proteins-I and -II from chicken egg yolk and their characterization. Biochem J 1995, 308:573-577.
    • (1995) Biochem. J. , vol.308 , pp. 573-577
    • Subramanian, N.1    Adiga, P.R.2
  • 10
    • 0024207480 scopus 로고
    • Purification and characterization of biotin-binding protein II from chicken oocytes
    • Bush L, McGahan TJ, White HB III: Purification and characterization of biotin-binding protein II from chicken oocytes. Biochem J 1988, 256:797-805.
    • (1988) Biochem. J. , vol.256 , pp. 797-805
    • Bush, L.1    McGahan, T.J.2    White III, H.B.3
  • 11
    • 0034684168 scopus 로고    scopus 로고
    • The lipocalin protein family: Structural and sequence overview
    • Flower DR, North AC, Sansom CE: The lipocalin protein family: structural and sequence overview. Biochim Biophys Acta 2000, 1482:9-24.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 9-24
    • Flower, D.R.1    North, A.C.2    Sansom, C.E.3
  • 12
    • 0034684227 scopus 로고    scopus 로고
    • Experimentally determined lipocalin structures
    • Flower DR: Experimentally determined lipocalin structures. Biochim Biophys Acta 2000, 1482:46-56.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 46-56
    • Flower, D.R.1
  • 13
    • 25444442086 scopus 로고    scopus 로고
    • Chicken genome
    • Chicken genome [http://www.genome.wustl.edu/projects/chicken/]
  • 18
    • 0019838202 scopus 로고
    • A chicken middle-repetitive DNA sequence which shares homology with mammalian ubiquitous repeats
    • Stumph WE, Kristo P, Tsai MJ, O'Malley BW: A chicken middle-repetitive DNA sequence which shares homology with mammalian ubiquitous repeats. Nucleic Acids Res 1981, 9:5383-5397.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 5383-5397
    • Stumph, W.E.1    Kristo, P.2    Tsai, M.J.3    O'Malley, B.W.4
  • 19
    • 0030579942 scopus 로고    scopus 로고
    • Two chicken repeat one (CR1) elements lacking a silencer-like region upstream of the chicken avidin-related genes Avr4 and Avr5
    • Wallén MJ, Keinänen RA, Kulomaa MS: Two chicken repeat one (CR1) elements lacking a silencer-like region upstream of the chicken avidin-related genes Avr4 and Avr5. Biochim Biophys Acta 1996, 1308:193-196.
    • (1996) Biochim. Biophys. Acta , vol.1308 , pp. 193-196
    • Wallén, M.J.1    Keinänen, R.A.2    Kulomaa, M.S.3
  • 21
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G: Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 1997, 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 22
    • 2442592993 scopus 로고    scopus 로고
    • A hidden markov model derived structural alphabet for proteins
    • Camproux AC, Gautier R, Tuffery P: A hidden markov model derived structural alphabet for proteins. J Mol Biol 2004, 339:591-605.
    • (2004) J. Mol. Biol. , vol.339 , pp. 591-605
    • Camproux, A.C.1    Gautier, R.2    Tuffery, P.3
  • 24
    • 0024588901 scopus 로고
    • Structural origins of high-affinity biotin binding to streptavidin
    • Weber PC, Ohlendorf DH, Wendoloski JJ, Salemme FR: Structural origins of high-affinity biotin binding to streptavidin. Science 1989, 243:85-88.
    • (1989) Science , vol.243 , pp. 85-88
    • Weber, P.C.1    Ohlendorf, D.H.2    Wendoloski, J.J.3    Salemme, F.R.4
  • 25
    • 0025286532 scopus 로고
    • Crystallographic refinement of human serum retinol binding protein at 2A resolution
    • Cowan SW, Newcomer ME, Jones TA: Crystallographic refinement of human serum retinol binding protein at 2A resolution. Proteins 1990, 8:44-61.
    • (1990) Proteins , vol.8 , pp. 44-61
    • Cowan, S.W.1    Newcomer, M.E.2    Jones, T.A.3
  • 29
    • 0347627526 scopus 로고    scopus 로고
    • Introduction of histidine residues into avidin subunit interfaces allows pH-dependent regulation of quaternary structure and biotin binding
    • Nordlund HR, Hytönen VP, Laitinen OH, Uotila ST, Niskanen EA, Savolainen J, Porkka E, Kulomaa MS: Introduction of histidine residues into avidin subunit interfaces allows pH-dependent regulation of quaternary structure and biotin binding. FEBS Lett 2003, 555:449-454.
    • (2003) FEBS Lett. , vol.555 , pp. 449-454
    • Nordlund, H.R.1    Hytönen, V.P.2    Laitinen, O.H.3    Uotila, S.T.4    Niskanen, E.A.5    Savolainen, J.6    Porkka, E.7    Kulomaa, M.S.8
  • 30
    • 0035955309 scopus 로고    scopus 로고
    • Copy-number fluctuation by unequal crossing-over in the chicken avidin gene family
    • Ahlroth MK, Ahlroth P, Kulomaa MS: Copy-number fluctuation by unequal crossing-over in the chicken avidin gene family. Biochem Bioph Res Co 2001, 288:400-406.
    • (2001) Biochem. Bioph. Res. Co. , vol.288 , pp. 400-406
    • Ahlroth, M.K.1    Ahlroth, P.2    Kulomaa, M.S.3
  • 32
    • 0032704893 scopus 로고    scopus 로고
    • Mutation of a critical tryptophan to lysine in avidin or streptavidin may explain why sea urchin fibropellin adopts an avidin-like domain
    • Laitinen OH, Airenne KJ, Marttila AT, Kulik T, Porkka E, Bayer EA, Wilchek M, Kulomaa MS: Mutation of a critical tryptophan to lysine in avidin or streptavidin may explain why sea urchin fibropellin adopts an avidin-like domain. FEBS Lett 1999, 461:52-58.
    • (1999) FEBS Lett. , vol.461 , pp. 52-58
    • Laitinen, O.H.1    Airenne, K.J.2    Marttila, A.T.3    Kulik, T.4    Porkka, E.5    Bayer, E.A.6    Wilchek, M.7    Kulomaa, M.S.8
  • 33
    • 0028938525 scopus 로고
    • Intersubunit contacts made by tryphtophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin
    • Sano T, Cantor CR: Intersubunit contacts made by tryphtophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin. Proc Natl Acad Sci USA 1995, 92:3180-3184.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3180-3184
    • Sano, T.1    Cantor, C.R.2
  • 35
    • 16544364808 scopus 로고    scopus 로고
    • Phylogeny and regulation of four lipocalin genes clustered in the chicken genome: Evidence of a functional diversification after gene duplication
    • Pagano A, Giannoni P, Zambotti A, Sanchez D, Ganfornina MD, Gutierrez G, Randazzo N, Cancedda R, Dozin B: Phylogeny and regulation of four lipocalin genes clustered in the chicken genome: evidence of a functional diversification after gene duplication. Gene 2004, 331:95-106.
    • (2004) Gene , vol.331 , pp. 95-106
    • Pagano, A.1    Giannoni, P.2    Zambotti, A.3    Sanchez, D.4    Ganfornina, M.D.5    Gutierrez, G.6    Randazzo, N.7    Cancedda, R.8    Dozin, B.9
  • 37
    • 4344650085 scopus 로고    scopus 로고
    • Construction of a dual chain pseudotetrameric chicken avidin by combining two circularly permuted avidins
    • Nordlund HR, Laitinen OH, Hytönen VP, Uotila ST, Porkka E, Kulomaa MS: Construction of a dual chain pseudotetrameric chicken avidin by combining two circularly permuted avidins. J Biol Chem 2004, 279:36715-36719.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36715-36719
    • Nordlund, H.R.1    Laitinen, O.H.2    Hytönen, V.P.3    Uotila, S.T.4    Porkka, E.5    Kulomaa, M.S.6
  • 38
    • 25444503280 scopus 로고    scopus 로고
    • Ensembl Chicken Genome Server
    • Ensembl Chicken Genome Server [http://www.ensembl.org/Gallus_gallus/]
  • 40
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment
    • Kumar S, Tamura K, Nei M: MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief Bioinform 2004, 5:150-63.
    • (2004) Brief Bioinform. , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 41
    • 0036166744 scopus 로고    scopus 로고
    • Dragon Promoter Finder: Recognition of vertebrate RNA polymerase II promoters
    • Bajic VB, Seah SH, Chong A, Zhang G, Koh JL, Brusic V: Dragon Promoter Finder: recognition of vertebrate RNA polymerase II promoters. Bioinformatics 2002, 18:198-9.
    • (2002) Bioinformatics , vol.18 , pp. 198-199
    • Bajic, V.B.1    Seah, S.H.2    Chong, A.3    Zhang, G.4    Koh, J.L.5    Brusic, V.6
  • 44
    • 0027305858 scopus 로고
    • Alignment and searching for common protein folds using a data bank of structural templates
    • Johnson MS, Overington JP, Blundell TL: Alignment and searching for common protein folds using a data bank of structural templates. J Mol Biol 1993, 231:735-752.
    • (1993) J. Mol. Biol. , vol.231 , pp. 735-752
    • Johnson, M.S.1    Overington, J.P.2    Blundell, T.L.3
  • 45
    • 25444473157 scopus 로고    scopus 로고
    • Structural Bioinformatics Laboratory: Bodil
    • Structural Bioinformatics Laboratory: Bodil.
  • 47
    • 0029884429 scopus 로고    scopus 로고
    • Discrimination of common protein folds: Application of protein structure to sequence/structure comparisons
    • Johnson MS, May AC, Rodionov MA, Overington JP: Discrimination of common protein folds: application of protein structure to sequence/structure comparisons. Method Enzymol 1996, 266:575-598.
    • (1996) Method Enzymol. , vol.266 , pp. 575-598
    • Johnson, M.S.1    May, A.C.2    Rodionov, M.A.3    Overington, J.P.4
  • 48
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL: Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993, 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 49
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton GJ: ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng 1993, 6:37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 51
    • 25444453768 scopus 로고    scopus 로고
    • SignalP 3.0 Server
    • SignalP 3.0 Server [http://www.cbs.dtu.dk/services/SignalP/]
  • 52
    • 25444512400 scopus 로고    scopus 로고
    • ExPASy-ProtParam tool
    • ExPASy-ProtParam tool [http://au.expasy.org/tools/protparam.html]
  • 53
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH: Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 1989, 182:319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 54
    • 25444473670 scopus 로고    scopus 로고
    • NetNGlyc 1.0 Server
    • NetNGlyc 1.0 Server [http://www.cbs.dtu.dk/services/NetNGlyc/]
  • 56
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment
    • Kumar S, Tamura K, Nei M: MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief Bioinform 2004, 5:150-63.
    • (2004) Brief Bioinform. , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.