메뉴 건너뛰기




Volumn 4, Issue 1, 2000, Pages 22-27

Role of linkers in communication between protein modules

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; POLYKETIDE SYNTHASE; PROTEIN TYROSINE KINASE;

EID: 0033982651     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)00046-0     Document Type: Review
Times cited : (173)

References (37)
  • 1
    • 0025825895 scopus 로고
    • Modular structure of transcription factors: Implications for gene regulation
    • Frankel A.D., Kim P.S. Modular structure of transcription factors: implications for gene regulation. Cell. 65:1991;717-719.
    • (1991) Cell , vol.65 , pp. 717-719
    • Frankel, A.D.1    Kim, P.S.2
  • 2
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen G.B., Ren R., Baltimore D. Modular binding domains in signal transduction proteins. Cell. 80:1995;237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 3
    • 0032488056 scopus 로고    scopus 로고
    • Imposing specificity by localization: Mechanism and evolvability
    • Ptashne M., Gann A. Imposing specificity by localization: mechanism and evolvability. Curr Biol. 8:1998;R897-R904.
    • (1998) Curr Biol , vol.8
    • Ptashne, M.1    Gann, A.2
  • 4
    • 0032541641 scopus 로고    scopus 로고
    • From Src homology domains to other signaling modules: Proposal of the 'protein recognition code'
    • Sudol M. From Src homology domains to other signaling modules: proposal of the 'protein recognition code'. Oncogene. 17:1998;1469-1474.
    • (1998) Oncogene , vol.17 , pp. 1469-1474
    • Sudol, M.1
  • 5
    • 0026415106 scopus 로고
    • Modular organization of genes required for complex polyketide biosynthesis
    • Donadio S., Staver M.J., McAlpine J.B., Swanson S.J., Katz L. Modular organization of genes required for complex polyketide biosynthesis. Science. 252:1991;675-679.
    • (1991) Science , vol.252 , pp. 675-679
    • Donadio, S.1    Staver, M.J.2    McAlpine, J.B.3    Swanson, S.J.4    Katz, L.5
  • 6
    • 0025081416 scopus 로고
    • An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea
    • Cortes J., Haydock S.F., Roberts G.A., Bevitt D.J., Leadlay P.F. An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea. Nature. 348:1990;176-178.
    • (1990) Nature , vol.348 , pp. 176-178
    • Cortes, J.1    Haydock, S.F.2    Roberts, G.A.3    Bevitt, D.J.4    Leadlay, P.F.5
  • 7
    • 9444278428 scopus 로고    scopus 로고
    • Modular peptide synthetases involved in nonribosomal peptide synthesis
    • Marahiel M.A., Stachelhaus T., Mootz H.D. Modular peptide synthetases involved in nonribosomal peptide synthesis. Chem Rev. 1997;2651-2673.
    • (1997) Chem Rev , pp. 2651-2673
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 8
    • 0033200367 scopus 로고    scopus 로고
    • Ligand recognition by SH3 and WW domains: The role of N-alkylation in PPII helices
    • Aghazadeh B., Rosen M.K. Ligand recognition by SH3 and WW domains: the role of N-alkylation in PPII helices. Chem Biol. 9:1999;R241-R246.
    • (1999) Chem Biol , vol.9
    • Aghazadeh, B.1    Rosen, M.K.2
  • 9
    • 0032775726 scopus 로고    scopus 로고
    • Src autoinhibition: Let us count the ways
    • Hubbard S.R. Src autoinhibition: let us count the ways. Nat Struct Biol. 8:1999;711-714.
    • (1999) Nat Struct Biol , vol.8 , pp. 711-714
    • Hubbard, S.R.1
  • 10
    • 0033596943 scopus 로고    scopus 로고
    • Flexibility of interdomain contacts revealed by topological isomers of bivalent consolidated ligands to the dual Src homology domain SH(32) of abelson
    • The flexibility of interdomain contacts between SH2 and SH3 domains has been investigated by synthesizing consolidated ligands, which combine the peptide sequences recognized by these two modules. This approach provides an alternative methodology to analyze the orientations of binding domains by designing ligands with multiple binding sites and topologies that would simultaneously bind to multiple sites.
    • Xu Q., Zheng J., Xu R., Barany G., Cowburn D. Flexibility of interdomain contacts revealed by topological isomers of bivalent consolidated ligands to the dual Src homology domain SH(32) of abelson. Biochemistry. 38:1999;3491-3497. The flexibility of interdomain contacts between SH2 and SH3 domains has been investigated by synthesizing consolidated ligands, which combine the peptide sequences recognized by these two modules. This approach provides an alternative methodology to analyze the orientations of binding domains by designing ligands with multiple binding sites and topologies that would simultaneously bind to multiple sites.
    • (1999) Biochemistry , vol.38 , pp. 3491-3497
    • Xu, Q.1    Zheng, J.2    Xu, R.3    Barany, G.4    Cowburn, D.5
  • 11
    • 0033543694 scopus 로고    scopus 로고
    • SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in rat-2 fibroblasts
    • This work provides compelling evidence that SH3 interactions with the SH2-kinase linker represent the dominant mechanism controlling Hck tyrosine kinase activity in vivo. The mutation of proline residues of the linker region causing the release of kinase and transforming activities.
    • Riggs S.D., Smithgall T.E. SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in rat-2 fibroblasts. J Biol Chem. 274:1999;26579-26583. This work provides compelling evidence that SH3 interactions with the SH2-kinase linker represent the dominant mechanism controlling Hck tyrosine kinase activity in vivo. The mutation of proline residues of the linker region causing the release of kinase and transforming activities.
    • (1999) J Biol Chem , vol.274 , pp. 26579-26583
    • Riggs, S.D.1    Smithgall, T.E.2
  • 12
    • 0033574768 scopus 로고    scopus 로고
    • Dissecting and exploiting intermodular communication in polyketide synthases
    • The role of linkers in mediating protein-protein interactions both within and between modules is described in this study. The transfer of biosynthetic intermediates between unnaturally linked modules was established by appropriate engineering of linkers. This approach renders a fundamentally new strategy for combinatorial biosynthesis in which individual modules are used as building blocks and linkers provide suitable module connectivity.
    • Gokhale R.S., Tsuji S.Y., Cane D.E., Khosla C. Dissecting and exploiting intermodular communication in polyketide synthases. Science. 284:1999;482-485. The role of linkers in mediating protein-protein interactions both within and between modules is described in this study. The transfer of biosynthetic intermediates between unnaturally linked modules was established by appropriate engineering of linkers. This approach renders a fundamentally new strategy for combinatorial biosynthesis in which individual modules are used as building blocks and linkers provide suitable module connectivity.
    • (1999) Science , vol.284 , pp. 482-485
    • Gokhale, R.S.1    Tsuji, S.Y.2    Cane, D.E.3    Khosla, C.4
  • 13
    • 0032077432 scopus 로고    scopus 로고
    • Insights into Src kinase functions: Structural comparisons
    • Williams J.C., Wierenga R.K., Saraste M. Insights into Src kinase functions: structural comparisons. Trends Biochem Sci. 5:1998;179-184.
    • (1998) Trends Biochem Sci , vol.5 , pp. 179-184
    • Williams, J.C.1    Wierenga, R.K.2    Saraste, M.3
  • 14
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • Xu W., Doshi A., Lei M., Eck M.J., Harrison S.C. Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol Cell. 5:1999;629-638.
    • (1999) Mol Cell , vol.5 , pp. 629-638
    • Xu, W.1    Doshi, A.2    Lei, M.3    Eck, M.J.4    Harrison, S.C.5
  • 15
    • 0033063429 scopus 로고    scopus 로고
    • Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor
    • Schindler T., Sicheri F., Pico A., Gazit A., Levitzki A., Kuriyan J. Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor. J Mol Cell. 5:1999;639-648.
    • (1999) J Mol Cell , vol.5 , pp. 639-648
    • Schindler, T.1    Sicheri, F.2    Pico, A.3    Gazit, A.4    Levitzki, A.5    Kuriyan, J.6
  • 16
    • 0032769397 scopus 로고    scopus 로고
    • Leucine 255 of Src couples intramolecular interactions to inhibition of catalysis
    • The involvement of the SH2-kinase linker in regulating intramolecular interactions between SH2 and SH3 is investigated in this paper. Mutation of Leu255 to various different hydrophobic residues revealed that the length and bulkiness of the side chain have profound influence on c-Src regulation.
    • Gonfloni S., Frischknecht F., Way M., Superti-Furga G. Leucine 255 of Src couples intramolecular interactions to inhibition of catalysis. Nat Struct Biol. 8:1999;760-764. The involvement of the SH2-kinase linker in regulating intramolecular interactions between SH2 and SH3 is investigated in this paper. Mutation of Leu255 to various different hydrophobic residues revealed that the length and bulkiness of the side chain have profound influence on c-Src regulation.
    • (1999) Nat Struct Biol , vol.8 , pp. 760-764
    • Gonfloni, S.1    Frischknecht, F.2    Way, M.3    Superti-Furga, G.4
  • 17
    • 0033610850 scopus 로고    scopus 로고
    • Intramolecular regulatory interactions in the Src family kinase Hck probed by mutagenesis of a conserved tryptophan residue
    • Mutation of Trp260 to alanine, which is a part of SH2-kinase linker and lies outside the poly-proline helix, activates the kinase domain, although, interestingly, the mutation was refractory to further activation through binding to either to SH2 or SH3 modules. This result suggested that Trp260 play a central role in coupling kinase and binding domains.
    • LaFevre-Bernt M., Sicheri F., Pico A., Porter M., Kuriyan J., Miller W.T. Intramolecular regulatory interactions in the Src family kinase Hck probed by mutagenesis of a conserved tryptophan residue. J Biol Chem. 273:1998;32129-32134. Mutation of Trp260 to alanine, which is a part of SH2-kinase linker and lies outside the poly-proline helix, activates the kinase domain, although, interestingly, the mutation was refractory to further activation through binding to either to SH2 or SH3 modules. This result suggested that Trp260 play a central role in coupling kinase and binding domains.
    • (1998) J Biol Chem , vol.273 , pp. 32129-32134
    • Lafevre-Bernt, M.1    Sicheri, F.2    Pico, A.3    Porter, M.4    Kuriyan, J.5    Miller, W.T.6
  • 18
    • 0032475992 scopus 로고    scopus 로고
    • Harnessing the biosynthetic code: Combinations, permutations, and mutations
    • Cane D.E., Walsh C.T., Khosla C. Harnessing the biosynthetic code: combinations, permutations, and mutations. Science. 282:1998;63-68.
    • (1998) Science , vol.282 , pp. 63-68
    • Cane, D.E.1    Walsh, C.T.2    Khosla, C.3
  • 20
    • 0001747786 scopus 로고    scopus 로고
    • Genetic contributions to understanding of polyketide synthases
    • Hopwood D.A. Genetic contributions to understanding of polyketide synthases. Chem Rev. 97:1997;2465-2497.
    • (1997) Chem Rev , vol.97 , pp. 2465-2497
    • Hopwood, D.A.1
  • 23
    • 0033515090 scopus 로고    scopus 로고
    • Multiple genetic modifications of the erythromycin polyketide synthase to produce a library of novel "unnatural" natural products
    • This study describes the state-of-the art technology for producing 'unnatural' natural products. The authors have engineered the erythromycin PKS genes to effect combinatorial alterations of catalytic activities, generating a library of more than 60 molecules
    • McDaniel R., Thamchaipenet A., Gustafsson C., Fu H., Betlach M., Ashley G. Multiple genetic modifications of the erythromycin polyketide synthase to produce a library of novel "unnatural" natural products. Proc Natl Acad Sci USA. 96:1999;1846-1851. This study describes the state-of-the art technology for producing 'unnatural' natural products. The authors have engineered the erythromycin PKS genes to effect combinatorial alterations of catalytic activities, generating a library of more than 60 molecules.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1846-1851
    • McDaniel, R.1    Thamchaipenet, A.2    Gustafsson, C.3    Fu, H.4    Betlach, M.5    Ashley, G.6
  • 24
    • 0032082090 scopus 로고    scopus 로고
    • Combinatorial biosynthesis for new drug discovery
    • Hutchinson C.R. Combinatorial biosynthesis for new drug discovery. Curr Opin Microbiol. 3:1998;319-329.
    • (1998) Curr Opin Microbiol , vol.3 , pp. 319-329
    • Hutchinson, C.R.1
  • 25
    • 0031197020 scopus 로고    scopus 로고
    • Combinatorial approaches to polyketide biosynthesis
    • Leadlay P.F. Combinatorial approaches to polyketide biosynthesis. Curr Opin Chem Biol. 2:1997;162-168.
    • (1997) Curr Opin Chem Biol , vol.2 , pp. 162-168
    • Leadlay, P.F.1
  • 26
    • 4244059507 scopus 로고    scopus 로고
    • Harnessing the biosynthetic potential of modular polyketide synthases
    • Khosla C. Harnessing the biosynthetic potential of modular polyketide synthases. Chem Rev. 97:1997;2577-2590.
    • (1997) Chem Rev , vol.97 , pp. 2577-2590
    • Khosla, C.1
  • 27
    • 0033529935 scopus 로고    scopus 로고
    • Direct evidence that the rifamycin polyketide synthase assembles polyketide chains processively
    • In this study, the rifF gene, which codes for an amide synthase, was inactivated in rifamycin PKS. This resulted in accumulation of a series of linear polyketides ranging from the tetraketide to the decaketide. This study provides strong evidence for the assembly-line operation of modular PKSs.
    • Yu T.W., Shen Y., Doi-Katayama Y., Tang L., Park C., Moore B.S., Hutchinson C.R., Floss H.G. Direct evidence that the rifamycin polyketide synthase assembles polyketide chains processively. Proc Natl Acad Sci USA. 96:1999;9051-9056. In this study, the rifF gene, which codes for an amide synthase, was inactivated in rifamycin PKS. This resulted in accumulation of a series of linear polyketides ranging from the tetraketide to the decaketide. This study provides strong evidence for the assembly-line operation of modular PKSs.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9051-9056
    • Yu, T.W.1    Shen, Y.2    Doi-Katayama, Y.3    Tang, L.4    Park, C.5    Moore, B.S.6    Hutchinson, C.R.7    Floss, H.G.8
  • 28
    • 0030875774 scopus 로고    scopus 로고
    • Precursor-directed biosynthesis of erythromycin analogs by an engineered polyketide synthase
    • Jacobsen J.R., Hutchinson C.R., Cane D.E., Khosla C. Precursor-directed biosynthesis of erythromycin analogs by an engineered polyketide synthase. Science. 277:1997;367-369.
    • (1997) Science , vol.277 , pp. 367-369
    • Jacobsen, J.R.1    Hutchinson, C.R.2    Cane, D.E.3    Khosla, C.4
  • 29
    • 0033591447 scopus 로고    scopus 로고
    • Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis
    • Kennedy J., Auclair K., Kendrew S.G., Park C., Vederas J.C., Hutchinson C.R. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science. 284:1999;1368-1372.
    • (1999) Science , vol.284 , pp. 1368-1372
    • Kennedy, J.1    Auclair, K.2    Kendrew, S.G.3    Park, C.4    Vederas, J.C.5    Hutchinson, C.R.6
  • 30
    • 0029856517 scopus 로고    scopus 로고
    • 6-deoxyerythronolide B synthase 1 is specifically acylated by a diketide intermediate at the beta-ketoacyl-acyl carrier protein synthase domain of module 2
    • Tsukamoto N., Chuck J.A., Luo G., Kao C.M., Khosla C., Cane D.E. 6-deoxyerythronolide B synthase 1 is specifically acylated by a diketide intermediate at the beta-ketoacyl-acyl carrier protein synthase domain of module 2. Biochemistry. 35:1996;15244-15248.
    • (1996) Biochemistry , vol.35 , pp. 15244-15248
    • Tsukamoto, N.1    Chuck, J.A.2    Luo, G.3    Kao, C.M.4    Khosla, C.5    Cane, D.E.6
  • 31
    • 0033215222 scopus 로고    scopus 로고
    • Knowledge-based design of bimodular and trimodular polyketide synthases based on domain and module swaps: A route to simple statin analogues
    • Transfer of intermediates between heterologous modules has been established by preserving the catalytic domains that are involved in protein-protein recognition. In this study, instead of only maintaining the linkers that mediate protein recognitions, the complete catalytic units were retained.
    • Ranganathan A., Timoney M., Bycroft M., Cortes J., Thomas I.P., Wilkinson B., Kellenberger L., Hanefeld U., Galloway I.S., Staunton J., Leadlay P.F. Knowledge-based design of bimodular and trimodular polyketide synthases based on domain and module swaps: a route to simple statin analogues. Chem Biol. 6:1999;731-741. Transfer of intermediates between heterologous modules has been established by preserving the catalytic domains that are involved in protein-protein recognition. In this study, instead of only maintaining the linkers that mediate protein recognitions, the complete catalytic units were retained.
    • (1999) Chem Biol , vol.6 , pp. 731-741
    • Ranganathan, A.1    Timoney, M.2    Bycroft, M.3    Cortes, J.4    Thomas, I.P.5    Wilkinson, B.6    Kellenberger, L.7    Hanefeld, U.8    Galloway, I.S.9    Staunton, J.10    Leadlay, P.F.11
  • 32
    • 0033079834 scopus 로고    scopus 로고
    • Mechanism and specificity of the terminal thioesterase domain from the erythromycin polyketide synthase
    • Gokhale R.S., Hunziker D., Cane D.E., Khosla C. Mechanism and specificity of the terminal thioesterase domain from the erythromycin polyketide synthase. Chem Biol. 2:1999;117-125.
    • (1999) Chem Biol , vol.2 , pp. 117-125
    • Gokhale, R.S.1    Hunziker, D.2    Cane, D.E.3    Khosla, C.4
  • 33
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas A. Coiled coils: new structures and new functions. Trends Biochem Sci. 10:1996;375-382.
    • (1996) Trends Biochem Sci , vol.10 , pp. 375-382
    • Lupas, A.1
  • 34
    • 0026073643 scopus 로고
    • Non-leucine residues in the leucine repeats of Fos and Jun contribute to the stability and determine the specificity of dimerization
    • Schuermann M., Hunter J.B., Hennig G., Muller R. Non-leucine residues in the leucine repeats of Fos and Jun contribute to the stability and determine the specificity of dimerization. Nucleic Acids Res. 19:1991;739-746.
    • (1991) Nucleic Acids Res , vol.19 , pp. 739-746
    • Schuermann, M.1    Hunter, J.B.2    Hennig, G.3    Muller, R.4
  • 35
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury P.B., Zhang T., Kim P.S., Alber T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science. 262:1993;1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 36
    • 0031460632 scopus 로고    scopus 로고
    • Influenza hemagglutinin is spring-loaded by a metastable native conformation
    • Carr C.M., Chaudhry C., Kim P.S. Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proc Natl Acad Sci USA. 94:1997;14306-14313.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14306-14313
    • Carr, C.M.1    Chaudhry, C.2    Kim, P.S.3
  • 37
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough P.A., Hughson F.M., Skehel J.J., Wiley D.C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature. 371:1994;37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.