The phosphorylation at Thr 124 of simian virus 40 large T antigen is crucial for its oligomerization
SV40 large T antigen is phosphorylated at up to ten different amino acids clustered in an N-terminal and a C-terminal part of the polypeptide chain. The N-terminal phosphorylated residues include Ser 123 and Thr 124. We have analyzed the oligomerization, the complex formation with the cellular oncop...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1987 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: FEBS Letters - Amsterdam : Elsevier, 221(1987), 2, Seite 199-204 |
| Übergeordnetes Werk: |
volume:221 ; year:1987 ; number:2 ; pages:199-204 |
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| 245 | 1 | 4 | |a The phosphorylation at Thr 124 of simian virus 40 large T antigen is crucial for its oligomerization |
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| 520 | |a SV40 large T antigen is phosphorylated at up to ten different amino acids clustered in an N-terminal and a C-terminal part of the polypeptide chain. The N-terminal phosphorylated residues include Ser 123 and Thr 124. We have analyzed the oligomerization, the complex formation with the cellular oncoprotein p53 and the DNA-binding properties of T antigen from two different SV40 transformed cell lines which have either an amino acid exchange at Ser 123 to Phe (W7) or Thr 124 to Ile (D29). In comparison to wild-type T antigen both mutant T antigens have a slightly reduced binding affinity for both binding sites, I and II, of SV40 DNA. Phosphorylation at both residues of T antigen is not essential for formation of the complex with p53. Only the phosphorylation at Thr 124 seems to be critical for the formation of high molecular mass oligomers. Our data support the hypothesis that the oligomerization of T antigen seems to be implicated in viral DNA replication. | ||
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(DE-627)NLEJ173175635 (DE-599)GBVNLZ173175635 DE-627 ger DE-627 rakwb eng The phosphorylation at Thr 124 of simian virus 40 large T antigen is crucial for its oligomerization 1987 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier SV40 large T antigen is phosphorylated at up to ten different amino acids clustered in an N-terminal and a C-terminal part of the polypeptide chain. The N-terminal phosphorylated residues include Ser 123 and Thr 124. We have analyzed the oligomerization, the complex formation with the cellular oncoprotein p53 and the DNA-binding properties of T antigen from two different SV40 transformed cell lines which have either an amino acid exchange at Ser 123 to Phe (W7) or Thr 124 to Ile (D29). In comparison to wild-type T antigen both mutant T antigens have a slightly reduced binding affinity for both binding sites, I and II, of SV40 DNA. Phosphorylation at both residues of T antigen is not essential for formation of the complex with p53. Only the phosphorylation at Thr 124 seems to be critical for the formation of high molecular mass oligomers. Our data support the hypothesis that the oligomerization of T antigen seems to be implicated in viral DNA replication. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Montenarh, M. oth Muller, D. oth in FEBS Letters Amsterdam : Elsevier 221(1987), 2, Seite 199-204 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:221 year:1987 number:2 pages:199-204 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(87)80925-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 221 1987 2 199-204 |
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(DE-627)NLEJ173175635 (DE-599)GBVNLZ173175635 DE-627 ger DE-627 rakwb eng The phosphorylation at Thr 124 of simian virus 40 large T antigen is crucial for its oligomerization 1987 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier SV40 large T antigen is phosphorylated at up to ten different amino acids clustered in an N-terminal and a C-terminal part of the polypeptide chain. The N-terminal phosphorylated residues include Ser 123 and Thr 124. We have analyzed the oligomerization, the complex formation with the cellular oncoprotein p53 and the DNA-binding properties of T antigen from two different SV40 transformed cell lines which have either an amino acid exchange at Ser 123 to Phe (W7) or Thr 124 to Ile (D29). In comparison to wild-type T antigen both mutant T antigens have a slightly reduced binding affinity for both binding sites, I and II, of SV40 DNA. Phosphorylation at both residues of T antigen is not essential for formation of the complex with p53. Only the phosphorylation at Thr 124 seems to be critical for the formation of high molecular mass oligomers. Our data support the hypothesis that the oligomerization of T antigen seems to be implicated in viral DNA replication. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Montenarh, M. oth Muller, D. oth in FEBS Letters Amsterdam : Elsevier 221(1987), 2, Seite 199-204 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:221 year:1987 number:2 pages:199-204 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(87)80925-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 221 1987 2 199-204 |
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(DE-627)NLEJ173175635 (DE-599)GBVNLZ173175635 DE-627 ger DE-627 rakwb eng The phosphorylation at Thr 124 of simian virus 40 large T antigen is crucial for its oligomerization 1987 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier SV40 large T antigen is phosphorylated at up to ten different amino acids clustered in an N-terminal and a C-terminal part of the polypeptide chain. The N-terminal phosphorylated residues include Ser 123 and Thr 124. We have analyzed the oligomerization, the complex formation with the cellular oncoprotein p53 and the DNA-binding properties of T antigen from two different SV40 transformed cell lines which have either an amino acid exchange at Ser 123 to Phe (W7) or Thr 124 to Ile (D29). In comparison to wild-type T antigen both mutant T antigens have a slightly reduced binding affinity for both binding sites, I and II, of SV40 DNA. Phosphorylation at both residues of T antigen is not essential for formation of the complex with p53. Only the phosphorylation at Thr 124 seems to be critical for the formation of high molecular mass oligomers. Our data support the hypothesis that the oligomerization of T antigen seems to be implicated in viral DNA replication. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Montenarh, M. oth Muller, D. oth in FEBS Letters Amsterdam : Elsevier 221(1987), 2, Seite 199-204 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:221 year:1987 number:2 pages:199-204 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(87)80925-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 221 1987 2 199-204 |
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(DE-627)NLEJ173175635 (DE-599)GBVNLZ173175635 DE-627 ger DE-627 rakwb eng The phosphorylation at Thr 124 of simian virus 40 large T antigen is crucial for its oligomerization 1987 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier SV40 large T antigen is phosphorylated at up to ten different amino acids clustered in an N-terminal and a C-terminal part of the polypeptide chain. The N-terminal phosphorylated residues include Ser 123 and Thr 124. We have analyzed the oligomerization, the complex formation with the cellular oncoprotein p53 and the DNA-binding properties of T antigen from two different SV40 transformed cell lines which have either an amino acid exchange at Ser 123 to Phe (W7) or Thr 124 to Ile (D29). In comparison to wild-type T antigen both mutant T antigens have a slightly reduced binding affinity for both binding sites, I and II, of SV40 DNA. Phosphorylation at both residues of T antigen is not essential for formation of the complex with p53. Only the phosphorylation at Thr 124 seems to be critical for the formation of high molecular mass oligomers. Our data support the hypothesis that the oligomerization of T antigen seems to be implicated in viral DNA replication. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Montenarh, M. oth Muller, D. oth in FEBS Letters Amsterdam : Elsevier 221(1987), 2, Seite 199-204 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:221 year:1987 number:2 pages:199-204 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(87)80925-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 221 1987 2 199-204 |
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(DE-627)NLEJ173175635 (DE-599)GBVNLZ173175635 DE-627 ger DE-627 rakwb eng The phosphorylation at Thr 124 of simian virus 40 large T antigen is crucial for its oligomerization 1987 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier SV40 large T antigen is phosphorylated at up to ten different amino acids clustered in an N-terminal and a C-terminal part of the polypeptide chain. The N-terminal phosphorylated residues include Ser 123 and Thr 124. We have analyzed the oligomerization, the complex formation with the cellular oncoprotein p53 and the DNA-binding properties of T antigen from two different SV40 transformed cell lines which have either an amino acid exchange at Ser 123 to Phe (W7) or Thr 124 to Ile (D29). In comparison to wild-type T antigen both mutant T antigens have a slightly reduced binding affinity for both binding sites, I and II, of SV40 DNA. Phosphorylation at both residues of T antigen is not essential for formation of the complex with p53. Only the phosphorylation at Thr 124 seems to be critical for the formation of high molecular mass oligomers. Our data support the hypothesis that the oligomerization of T antigen seems to be implicated in viral DNA replication. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Montenarh, M. oth Muller, D. oth in FEBS Letters Amsterdam : Elsevier 221(1987), 2, Seite 199-204 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:221 year:1987 number:2 pages:199-204 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(87)80925-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 221 1987 2 199-204 |
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phosphorylation at thr 124 of simian virus 40 large t antigen is crucial for its oligomerization |
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The phosphorylation at Thr 124 of simian virus 40 large T antigen is crucial for its oligomerization |
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SV40 large T antigen is phosphorylated at up to ten different amino acids clustered in an N-terminal and a C-terminal part of the polypeptide chain. The N-terminal phosphorylated residues include Ser 123 and Thr 124. We have analyzed the oligomerization, the complex formation with the cellular oncoprotein p53 and the DNA-binding properties of T antigen from two different SV40 transformed cell lines which have either an amino acid exchange at Ser 123 to Phe (W7) or Thr 124 to Ile (D29). In comparison to wild-type T antigen both mutant T antigens have a slightly reduced binding affinity for both binding sites, I and II, of SV40 DNA. Phosphorylation at both residues of T antigen is not essential for formation of the complex with p53. Only the phosphorylation at Thr 124 seems to be critical for the formation of high molecular mass oligomers. Our data support the hypothesis that the oligomerization of T antigen seems to be implicated in viral DNA replication. |
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SV40 large T antigen is phosphorylated at up to ten different amino acids clustered in an N-terminal and a C-terminal part of the polypeptide chain. The N-terminal phosphorylated residues include Ser 123 and Thr 124. We have analyzed the oligomerization, the complex formation with the cellular oncoprotein p53 and the DNA-binding properties of T antigen from two different SV40 transformed cell lines which have either an amino acid exchange at Ser 123 to Phe (W7) or Thr 124 to Ile (D29). In comparison to wild-type T antigen both mutant T antigens have a slightly reduced binding affinity for both binding sites, I and II, of SV40 DNA. Phosphorylation at both residues of T antigen is not essential for formation of the complex with p53. Only the phosphorylation at Thr 124 seems to be critical for the formation of high molecular mass oligomers. Our data support the hypothesis that the oligomerization of T antigen seems to be implicated in viral DNA replication. |
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SV40 large T antigen is phosphorylated at up to ten different amino acids clustered in an N-terminal and a C-terminal part of the polypeptide chain. The N-terminal phosphorylated residues include Ser 123 and Thr 124. We have analyzed the oligomerization, the complex formation with the cellular oncoprotein p53 and the DNA-binding properties of T antigen from two different SV40 transformed cell lines which have either an amino acid exchange at Ser 123 to Phe (W7) or Thr 124 to Ile (D29). In comparison to wild-type T antigen both mutant T antigens have a slightly reduced binding affinity for both binding sites, I and II, of SV40 DNA. Phosphorylation at both residues of T antigen is not essential for formation of the complex with p53. Only the phosphorylation at Thr 124 seems to be critical for the formation of high molecular mass oligomers. Our data support the hypothesis that the oligomerization of T antigen seems to be implicated in viral DNA replication. |
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