메뉴 건너뛰기




Volumn 1, Issue 3, 1997, Pages 292-299

Protein splicing and autoproteolysis mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

ERINACEIDAE;

EID: 0031244525     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(97)80065-8     Document Type: Article
Times cited : (140)

References (30)
  • 1
    • 0030763705 scopus 로고    scopus 로고
    • Compilation and analysis of intein sequences
    • Perler FB, Olsen GJ, Adam E: Compilation and analysis of intein sequences. Nucleic Acids Res 1997, 25:1087-1093. This catalog lists published intein sequences, as well as the phylogenetic relationships among inteins. A new intein motif, Block H, is described and the intein motifs first defined in [13] are listed for all inteins. An updated intein database is maintained on the New England Biolabs Web site (http://www.neb.com/).
    • (1997) Nucleic Acids Res , vol.25 , pp. 1087-1093
    • Perler, F.B.1    Olsen, G.J.2    Adam, E.3
  • 2
    • 0041990223 scopus 로고
    • A search for specific chemical methods for fission of peptide bonds. 1. The N-acyl to O-acyl transformation in the degradation of silk fibroin
    • Elliott DF: A search for specific chemical methods for fission of peptide bonds. 1. The N-acyl to O-acyl transformation in the degradation of silk fibroin. Biochem J 1952, 50:542-550.
    • (1952) Biochem J , vol.50 , pp. 542-550
    • Elliott, D.F.1
  • 3
    • 0029923954 scopus 로고    scopus 로고
    • From peptide precursors to oxazole and thiazole-containing peptide antibiotics: Microcin B17 synthase
    • Li YM, Milne JC, Madison LL, Kolter R, Walsh CT: From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase. Science 1996, 274:1188-1193.
    • (1996) Science , vol.274 , pp. 1188-1193
    • Li, Y.M.1    Milne, J.C.2    Madison, L.L.3    Kolter, R.4    Walsh, C.T.5
  • 4
    • 0029838842 scopus 로고    scopus 로고
    • The mechanism of protein splicing and its modulation by mutation
    • Xu M-Q, Perler FB: The mechanism of protein splicing and its modulation by mutation. EMBO J 1996, 15:5146-5153. Mutation of conserved splice junction residues of the Psp pol-1 intein defines the roles of each residue. A cold-sensitive mutation allows splicing at temperatures of 37°C or above, but not below 37°C. The rate of hydrolysis at the amino-terminal splice junction in MBP-intein fusions is 10-fold higher if a serine is also present at the carboxy-terminal splice junction. The presence of the linear ester intermediate in a precursor containing a Ser-1→Cys mutation is confirmed by cleavage with hydroxylamine, free cysteine or dithiothreitol.
    • (1996) EMBO J , vol.15 , pp. 5146-5153
    • Xu, M.-Q.1    Perler, F.B.2
  • 5
    • 0030012109 scopus 로고    scopus 로고
    • Protein splicing: Evidence for an N-O acyl rearrangement as the initial step in the splicing process
    • Shao Y, Xu M-Q, Paulus H: Protein splicing: evidence for an N-O acyl rearrangement as the initial step in the splicing process. Biochemistry 1996, 35:3810-3815. Provides evidence for a linear ester intermediate by demonstrating cleavage by hydroxylamine and by identifying the N-extein carboxy-terminal hydroxamate using mass spectrometry and a colorimetric assay for hydroxamic acids.
    • (1996) Biochemistry , vol.35 , pp. 3810-3815
    • Shao, Y.1    Xu, M.-Q.2    Paulus, H.3
  • 6
    • 0030051163 scopus 로고    scopus 로고
    • Activation of glycosylasparaginase. Formation of active N-terminal threonine by intramolecular autoproteolysis
    • Guan C, Cui T, Rao V, Liao W, Benner J, Lin CL, Comb D: Activation of glycosylasparaginase. Formation of active N-terminal threonine by intramolecular autoproteolysis. J Biol Chem 1996, 271:1732-1737. Describes the isolation of the bacterial glycosylasparaginase precursor and its processing in vivo.
    • (1996) J Biol Chem , vol.271 , pp. 1732-1737
    • Guan, C.1    Cui, T.2    Rao, V.3    Liao, W.4    Benner, J.5    Lin, C.L.6    Comb, D.7
  • 7
    • 0029834656 scopus 로고    scopus 로고
    • Protein splicing involving the Saccharomyces cerevisiae VMA intein: The steps in the splicing pathway, side reactions leading to protein cleavage, and establishment of an in vitro splicing system
    • Chong S, Shao Y, Paulus H, Benner J, Perler FB, Xu MQ: Protein splicing involving the Saccharomyces cerevisiae VMA intein: the steps in the splicing pathway, side reactions leading to protein cleavage, and establishment of an in vitro splicing system. J Biol Chem 1996, 271:22159-22168. The mesophilic Saccharomyces cerevisiae VMA intein, bounded by cysteine residues, splices by the same pathway described for the thermostable Psp pol-1 intein bounded by serine residues. Several lines of evidence demonstrate the occurrence of a thioester intermediate. Labeling of the carboxyl terminus of the upstream extein by radioactive cysteine is described, as are mutations that allow controllable cleavage at the intein amino terminus by thiols.
    • (1996) J Biol Chem , vol.271 , pp. 22159-22168
    • Chong, S.1    Shao, Y.2    Paulus, H.3    Benner, J.4    Perler, F.B.5    Xu, M.Q.6
  • 8
    • 15844386540 scopus 로고    scopus 로고
    • Hedgehog patterning activity: Role of lipophilic modification mediated by the carboxy-terminal autoprocessing domain
    • Porter JA, Ekker SC, Park WJ, von Kessler DP, Young KE, Chen CH, Ma Y, Woods AS, Cotter RJ, Koonin EV, Beachy PA: Hedgehog patterning activity: role of lipophilic modification mediated by the carboxy-terminal autoprocessing domain. Cell 1996, 86:21-34. This paper reports groundbreaking studies that demonstrate that the hedgehog protein (Hh) signaling domain is modified by addition of a lipid group during autoprocessing. The absence of lipid inactivates the hedgehog protein signaling domain by preventing its accumulation in the outer membrane. The Hh carboxyl domain (Hh-C) contains sufficient information for lipid addition. The authors identify several proteins with similarity to Hh-C and cysteine-dependent cleavage in one of these proteins is demonstrated. The authors suggest that Drosophila Hh residues Cys258, His329 and Asp282 are conserved in Hh-C-related proteins and constitute the autoproteolytic catalytic triad.
    • (1996) Cell , vol.86 , pp. 21-34
    • Porter, J.A.1    Ekker, S.C.2    Park, W.J.3    Von Kessler, D.P.4    Young, K.E.5    Chen, C.H.6    Ma, Y.7    Woods, A.S.8    Cotter, R.J.9    Koonin, E.V.10    Beachy, P.A.11
  • 11
    • 0027984269 scopus 로고
    • Protein splicing: An analysis of the branched intermediate and its resolution by succinimide formation
    • Xu M-Q, Comb DG, Paulus H, Noren CJ, Shao Y, Perler FB: Protein splicing: An analysis of the branched intermediate and its resolution by succinimide formation. EMBO J 1994, 13:5517-5522.
    • (1994) EMBO J , vol.13 , pp. 5517-5522
    • Xu, M.-Q.1    Comb, D.G.2    Paulus, H.3    Noren, C.J.4    Shao, Y.5    Perler, F.B.6
  • 12
    • 0029844192 scopus 로고    scopus 로고
    • Cholesterol modification of hedgehog signaling proteins in animal development
    • Porter JA, Young KE, Beachy PA: Cholesterol modification of hedgehog signaling proteins in animal development. Science 1996, 274:255-259. This paper identifies the lipid adduct on the hedgehog protein amino domain (Hh-N) as cholesterol and positions it at the carboxyl terminus of the Hh signaling domain. The absence of cholesterol inactivates the Hh protein signaling domain and prevents its accumulation at the cell surface. Cholesterol is covalently attached to Hh-N by an alkali labile linkage, suggesting that the cholesterol moiety is linked to Hh-N by an ester bond. Cholesterol is found on amino domains of hedgehog proteins in the cells of many species, from monkey to mouse.
    • (1996) Science , vol.274 , pp. 255-259
    • Porter, J.A.1    Young, K.E.2    Beachy, P.A.3
  • 13
    • 0028607524 scopus 로고
    • Conserved sequence features of inteins (protein introns) and their use in identifying new inteins and related proteins
    • Pietrokovski S: Conserved sequence features of inteins (protein introns) and their use in identifying new inteins and related proteins. Protein Sci 1994, 3:2340-2350.
    • (1994) Protein Sci , vol.3 , pp. 2340-2350
    • Pietrokovski, S.1
  • 14
    • 0027315426 scopus 로고
    • Protein splicing of the yeast TFP1 intervening protein sequence: A model for self-excision
    • Cooper AA, Chen Y-J, Lindorfer MA, Stevens TH: Protein splicing of the yeast TFP1 intervening protein sequence: a model for self-excision. EMBO J 1993, 12:2575-2583.
    • (1993) EMBO J , vol.12 , pp. 2575-2583
    • Cooper, A.A.1    Chen, Y.-J.2    Lindorfer, M.A.3    Stevens, T.H.4
  • 15
    • 0026774103 scopus 로고
    • Protein splicing in the maturation of M. tuberculosis Reca protein: A mechanism for tolerating a novel class of intervening sequence
    • Davis EO, Jenner PJ, Brooks PC, Colston MJ, Sedgwick SG: Protein splicing in the maturation of M. tuberculosis RecA protein: A mechanism for tolerating a novel class of intervening sequence. Cell 1992, 71:201-210.
    • (1992) Cell , vol.71 , pp. 201-210
    • Davis, E.O.1    Jenner, P.J.2    Brooks, P.C.3    Colston, M.J.4    Sedgwick, S.G.5
  • 16
    • 0026462996 scopus 로고
    • +-ATPase, inhibit its processing by protein splicing
    • +-ATPase, inhibit its processing by protein splicing. Biochem Biophys Res Commun 1992, 188:40-47.
    • (1992) Biochem Biophys Res Commun , vol.188 , pp. 40-47
    • Hirata, R.1    Anraku, Y.2
  • 17
    • 0027051618 scopus 로고
    • Protein splicing removes intervening sequences in an archaea DNA polymerase
    • Hodges RA, Perler FB, Noren CJ, Jack WE: Protein splicing removes intervening sequences in an archaea DNA polymerase. Nucleic Acids Res 1992, 20:6153-6157.
    • (1992) Nucleic Acids Res , vol.20 , pp. 6153-6157
    • Hodges, R.A.1    Perler, F.B.2    Noren, C.J.3    Jack, W.E.4
  • 18
    • 0027753790 scopus 로고
    • In vitro protein splicing of purified precursor and the identification of a branched intermediate
    • Xu M-Q, Southworth MW, Mersha FB, Hornstra LJ, Perler FB: In vitro protein splicing of purified precursor and the identification of a branched intermediate. Cell 1993, 75:1371-1377.
    • (1993) Cell , vol.75 , pp. 1371-1377
    • Xu, M.-Q.1    Southworth, M.W.2    Mersha, F.B.3    Hornstra, L.J.4    Perler, F.B.5
  • 19
    • 0028080347 scopus 로고
    • A proposed mechanism for the self-splicing of proteins
    • Clarke ND: A proposed mechanism for the self-splicing of proteins. Proc Natl Acad Sci USA 1994, 91:11084-11088.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11084-11088
    • Clarke, N.D.1
  • 20
    • 0001921138 scopus 로고
    • Deamidation and isoaspartate formation in model synthetic peptides: The effects of sequence and solution environment
    • Edited by Aswad DW. Boca Raton: CRC Press
    • Brennan TV, Clarke S: Deamidation and isoaspartate formation in model synthetic peptides: The effects of sequence and solution environment. In Deamidation and Isoaspartate Formation in Peptides and Proteins. Edited by Aswad DW. Boca Raton: CRC Press; 1995:65-90.
    • (1995) Deamidation and Isoaspartate Formation in Peptides and Proteins , pp. 65-90
    • Brennan, T.V.1    Clarke, S.2
  • 21
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation
    • Geiger T, Clarke S: Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J Biol Chem 1987, 262:785-794.
    • (1987) J Biol Chem , vol.262 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 22
    • 0029124041 scopus 로고
    • Protein splicing: Characterization of the aminosuccinimide residue at the carboxyl terminus of the excised intervening sequence
    • Shao Y, Xu M-Q, Paulus H: Protein splicing: characterization of the aminosuccinimide residue at the carboxyl terminus of the excised intervening sequence. Biochemistry 1995, 34:10844-10850.
    • (1995) Biochemistry , vol.34 , pp. 10844-10850
    • Shao, Y.1    Xu, M.-Q.2    Paulus, H.3
  • 23
    • 0029936212 scopus 로고    scopus 로고
    • Functional analyses of the active site residues of human lysosomal aspartylglucosaminidase: Implications for catalytic mechanism and autocatalytic activation
    • Tikkanen R, Riikonen A, Oinonen C, Rouvinen J, Peltonen L: Functional analyses of the active site residues of human lysosomal aspartylglucosaminidase: implications for catalytic mechanism and autocatalytic activation. EMBO J 1996, 15:2954-2960.
    • (1996) EMBO J , vol.15 , pp. 2954-2960
    • Tikkanen, R.1    Riikonen, A.2    Oinonen, C.3    Rouvinen, J.4    Peltonen, L.5
  • 24
    • 0028842195 scopus 로고
    • Molecular cloning and sequence analysis of Flavobacterium meningosepticum glycosylasparaginase: A single gene encodes the α and β subunits
    • Tarentino AL, Quinones G, Hauer CR, Changchien LM, Plummer TH: Molecular cloning and sequence analysis of Flavobacterium meningosepticum glycosylasparaginase: a single gene encodes the α and β subunits. Arch Biochem Biophys 1995, 316:399-406.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 399-406
    • Tarentino, A.L.1    Quinones, G.2    Hauer, C.R.3    Changchien, L.M.4    Plummer, T.H.5
  • 26
    • 0027389271 scopus 로고
    • Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum
    • Ikonen E, Julkunen I, Tollersrud OK, Kalkkinen N, Peltonen L: Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum. EMBO J 1993, 12:295-302.
    • (1993) EMBO J , vol.12 , pp. 295-302
    • Ikonen, E.1    Julkunen, I.2    Tollersrud, O.K.3    Kalkkinen, N.4    Peltonen, L.5
  • 28
    • 0028944672 scopus 로고
    • A protein splice-junction motif in hedgehog family proteins
    • Koonin EV: A protein splice-junction motif in hedgehog family proteins. Trends Biochem Sci 1995, 20:141-142.
    • (1995) Trends Biochem Sci , vol.20 , pp. 141-142
    • Koonin, E.V.1
  • 29


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.