Biochemical and NMR spectroscopic investigations on the Hsp90 chaperone system:
Gespeichert in:
| 1. Verfasser: | |
|---|---|
| Format: | Abschlussarbeit Buch |
| Sprache: | English |
| Veröffentlicht: |
2012
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| Schlagworte: | |
| Online-Zugang: | Volltext https://nbn-resolving.org/urn:nbn:de:bvb:91-diss-20120612-1099102-0-9 Inhaltsverzeichnis |
| Beschreibung: | XXXVIII, 532 S. graph. Darst. |
Internformat
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| 245 | 1 | 0 | |a Biochemical and NMR spectroscopic investigations on the Hsp90 chaperone system |c Stephan Lagleder |
| 264 | 1 | |c 2012 | |
| 300 | |a XXXVIII, 532 S. |b graph. Darst. | ||
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| 502 | |a München, Techn. Univ., Diss., 2012 | ||
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Datensatz im Suchindex
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| adam_text | IMAGE 1
TABLE O F CONTENTS
LIST OF FIGURES IX
LIST OF TABLES XXIII
ABBREVIATIONS AND SYMBOLS XXIX
SCOPE OF THIS WORK XXXVII
I INTRODUCTION 1
1 THE HSP90 MOLECULAR CHAPERONE 3
1.1 CONSERVATION OF THE HSP90 CHAPERONE SYSTEM 3
1.2 HSP90 STRUCTURE 7
1.3 HSP90 ATPASE ACTIVITY AND CHAPERONE CYCLE 11
1.4 HSP90 CHAPERONE ACTIVITY 19
2 HSP90 COCHAPERONES 25
2.1 STIL/HOP 25
2.1.1 FUNCTIONS OF STIL/HOP IN THE HSP70-HSP90 SYSTEM 25
2.1.2 DOMAIN STRUCTURE OF STIL/HOP 27
2.1.3 STIL/HOP TETRATRICOPEPTIDE REPEAT (TPR) DOMAINS 28
2.1.4 STIL/HOP DP DOMAINS 37
2.2 AHAL/HCHL 40
HTTP://D-NB.INFO/1034437259
IMAGE 2
II
TABLE O F CONTENTS
2.3 P23/SBAL 44
II RESULTS 49
3 ANALYSIS OF HSP90 - CLIENT PROTEIN COMPLEXES 51 3.1 BINDING AFFINITIES
OF ISOLATED HSP90 DOMAINS AND P53 DBD 51 3.2 NMR BACKBONE ASSIGNMENT OF
THE HSP90 CA20 MUTANT . . 62
3.3 FAST BACKBONE DYNAMICS OF HSP90 CA20 74
3.4 NMR BINDING STUDIES WITH HSP90 CA20 AND P53 DBD . . . 76
3.5 MOLECULAR DOCKING OF THE HSP90 CA20 - P 5 3 DBD COMPLEX 88
3.6 VALIDATION OF P53 DBD BINDING SITES ON HSP90 BY MUTAGE NESIS 96
3.7 CLIENT PROTEIN BINDING AND HSP90 CHAPERONE CYCLE 102
3.8 HSP90 C DOMAIN MUTANTS AND P53 IN VIVO ACTIVITY 107
3.9 CHAPERONING OF P53 DBD BY HSP90 112
3.10 INTERACTIONS OF HSP90 WITH A - SYNUCLEIN 121
3.11 DISCUSSION 127
4 THE HSP90 COCHAPERONE STIL 133
4.1 DESIGN AND CD CHARACTERIZATION OF STIL TPR DOMAINS . . . . 133 4.2
DESIGN AND CD CHARACTERIZATION OF HSP70/SSAL FRAGMENTS 142
4.3 PEPTIDE BINDING SELECTIVITY OF STIL TPR DOMAINS 144
4.4 NMR CHARACTERIZATION OF STIL TPR DOMAINS 163
4.4.1 NMR BACKBONE ASSIGNMENT OF STIL TPR DOMAINS . . 163
4.4.2 NMR STRUCTURE DETERMINATION OF THE STIL TPR2B
DOMAIN 170
4.4.3 FAST BACKBONE DYNAMICS OF STIL TPR DOMAINS . . . . 182
4.4.4 THE OLIGOMERIC STATE OF STIL TPR DOMAINS 183
IMAGE 3
TABLE O F CONTENTS III
4.4.5 PEPTIDE BINDING OF STDL TPR DOMAINS MONITORED BY
NMR 188
4.5 CHARACTERIZATION OF STNL PEPTIDE BINDING MUTANTS 202
4.6 INFLUENCE OF STIL ON THE HSP90 ATPASE ACTIVITY 206
4.7 PEPTIDE INDEPENDENT BINDING CONTACTS OF STIL WITH HSP90 . 212
4.8 PEPTIDE INDEPENDENT BINDING CONTACTS OF STIL WITH HSP70 . 218 4.9
FORMATION OF STIL/HSP70/HSP90 TERNARY COMPLEXES . . . . 224
4.10 ANALYSIS OF A STIL TPR2A-TPR2B LINKER MUTANT 228
4.11 IN VIVO ANALYSIS OF STIL TPR DOMAIN MUTANTS 233
4.12 NMR DOCKING OF STIL TPR2A - TPR2B AND HSP90 238
4.13 SCREENING FOR INHIBITORS OF THE STIL PEPTIDE BINDING 258
4.14 STRUCTURAL CHARACTERIZATION OF STIL DP DOMAINS 275 4.14.1
CHARACTERIZATION OF INITIAL DP DOMAIN CONSTRUCTS . . 275 4.14.2
CONSTRUCT OPTIMIZATION AND NMR BACKBONE ASSIGN
MENT OF STIL DP DOMAINS 277
4.14.3 NMR STRUCTURE DETERMINATION OF STIL DP DOMAINS . 287
4.14.4 FAST BACKBONE DYNAMICS OF STIL DP DOMAINS . . . . 307
4.15 IN VIVO FUNCTION OF STIL DP DOMAINS 308
4.16 BINDING STUDIES WITH STIL DP DOMAINS 316
4.17 ANALYSIS OF STIL TPR - DP FRAGMENTS 322
4.18 DISCUSSION 334
4.18.1 THE ROLE OF THE TPR SOLUBILITY HELIX 334
4.18.2 PEPTIDE BINDING SELECTIVITIES OF STIL TPR DOMAINS . 336
4.18.3 TPR2B STRUCTURE DETERMINATION 341
4.18.4 PEPTIDE BINDING PROPERTIES OF THE STIL TPR2A AND
TPR2B DOMAINS IN SOLUTION 344
4.18.5 INFLUENCE OF STIL ON THE HSP90 ATPASE ACTIVITY . . . 347 4.18.6
PEPTIDE INDEPENDENT BINDING CONTACTS OF STIL WITH
HSP70 AND HSP90 349
IMAGE 4
TABLE O F CONTENTS
4.18.7 TERNARY COMPLEXES BETWEEN STIL, HSP70 AND HSP90 354
4.18.8 THE ROLE OF THE LINKER BETWEEN THE STIL TPR2A AND
TPR2B DOMAIN 356
4.18.9 IN VIVO FUNCTION OF STIL TPR DOMAIN MUTANTS . . . . 359
4.18.10 THE COMPLEX BETWEEN HSP90 AND STIL 361
4.18.11 SCREENING FOR TPR DOMAIN INHIBITORS 369
4.18.12 THE DP DOMAIN STRUCTURES 374
4.18.13 POTENTIAL FUNCTIONS OF STIL/HOP DP DOMAINS . . . 377
5 THE HSP90 COCHAPERONE HCHL 383
5.1 EXPRESSION AND PURIFICATION OF HCHL 383
5.2 STRUCTURAL CHARACTERIZATION OF HCHL 386
5.3 COMPLEX FORMATION OF HCHL AND HSP90 393
5.4 DISCUSSION 402
6 THE HSP90 COCHAPERONE SBAL 407
6.1 INITIAL STRUCTURAL CHARACTERIZATION OF SBAL FARIANTS 407 6.2
STRUCTURE PROPENSITY OF THE SBAL C DOMAIN 412
6.3 NMR BACKBONE ASSIGNMENT OF THE SBAL N DOMAIN 417
6.4 MODEL BUILDING FOR THE SBAL N DOMAIN IN SOLUTION 421
6.5 FAST BACKBONE DYNAMICS OF THE SBAL N DOMAIN 426
6.6 COMPLEX FORMATION OF SBAL AND HSP90 427
6.7 CHAPERONE ACTIVITY OF SBAL 434
6.8 DISCUSSION 437
III EXPERIMENTAL SECTION 441
7 MOLECULAR BIOLOGY 443
7.1 POLYMERASE CHAIN REACTION 443
IMAGE 5
TABLE O F CONTENTS V
7.2 PLASMID DNA ISOLATION AND DNA FRAGMENT PURIFICATION . . . 445
7.3 OLIGONUCLEOTIDES 446
7.4 DNA MANIPULATION 452
7.5 MUTAGENESIS OF DNA 452
7.6 AGAROSE GEL ELECTROPHORESIS 453
7.7 DNA SEQUENCING 454
8 CELL CULTURE 455
8.1 CELL STRAINS 455
8.2 MEDIA FOR GROWING CELLS 456
8.3 PREPARATION OF COMPETENT CELLS 457
8.4 TRANSFORMATION OF CELLS 457
8.5 LONG TERM STORAGE OF CELLS 458
8.6 PREPARATION OF E. COLI PROTEIN EXPRESSION CULTURES 458
9 PROTEIN EXPRESSION AND PURIFICATION 461
9.1 PREPARATION OF CELL EXTRACTS 461
9.2 PREPARATION OF INCLUSION BODIES 462
9.3 REFOLDING OF PROTEINS 463
9.4 FAST PROTEIN LIQUID CHROMATOGRAPHY 464
9.4.1 AFFINITY CHROMATOGRAPHY 464
9.4.2 ANION EXCHANGE CHROMATOGRAPHY 466
9.4.3 CATION EXCHANGE CHROMATOGRAPHY 467
9.4.4 HYDROXYLAPATITE CHROMATOGRAPHY 467
9.4.5 GELFILTRATION CHROMATOGRAPHY 468
9.4.6 DESALTING/BUFFER EXCHANGE 468
9.5 CONCENTRATION OF PROTEINS 469
9.6 PROTEIN DIGEST WITH THROMBIN 469
9.7 EXPRESSION AND PURIFICATION OF HSP90 CONSTRUCTS 470
IMAGE 6
VI
TABLE O F CONTENTS
9.8 EXPRESSION AND PURIFICATION OF P53 DBD 472
9.9 EXPRESSION AND PURIFICATION OF STIL CONSTRUCTS 473
9.10 EXPRESSION AND PURIFICATION OF HSP70/SSAL FRAGMENTS . . . 475
9.11 EXPRESSION AND PURIFICATION OF HCHL 476
9.12 EXPRESSION AND PURIFICATION OF SBAL CONSTRUCTS 476
10 PROTEIN ANALYSIS 479
10.1 SDS - PAGE 479
10.2 DETERMINATION OF PROTEIN CONCENTRATION 481
10.3 CHEMICAL CROSSLINKING 481
10.4 UV/VIS SPECTROSCOPY 481
10.5 CD SPECTROSCOPY 482
10.6 ATPASE ACTIVITY ASSAY 482
10.7 THERMOFLUOR STABILITY ASSAY 482
10.8 ISOTHERMAL TITRATION CALORIMETRY 483
10.9 SURFACE PLASMON RESONANCE 484
10.10 CHAPERONE ASSAY 484
10.11 FLUORESCENCE POLARIZATION BINDING ASSAYS 485
10.12 ANALYTICAL GELFILTRATION 486
10.13 NMR SPECTROSCOPY 486
10.13.1 PROTEIN RESONANCE ASSIGNMENT 486
10.13.2 NMR CHEMICAL SHIFT PERTURBATION EXPERIMENTS. . . 487
10.13.3 EXTRACTION OF BINDING AFFINITIES FROM NMR DATA . . 487
10.13.4 PRE EXPERIMENTS 488
11 SOFTWARE 489
IMAGE 7
TABLE O F CONTENTS
I V APPENDIX
CHEMICAL SHIFT LISTS
SUMMARY
ZUSAMMENFASSUNG
BIBLIOGRAPHY
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| spelling | Lagleder, Stephan Verfasser aut Biochemical and NMR spectroscopic investigations on the Hsp90 chaperone system Stephan Lagleder 2012 XXXVIII, 532 S. graph. Darst. txt rdacontent n rdamedia nc rdacarrier München, Techn. Univ., Diss., 2012 Hitzeschock-Proteine (DE-588)4255487-1 gnd rswk-swf Biochemie (DE-588)4006777-4 gnd rswk-swf NMR-Spektroskopie (DE-588)4075421-2 gnd rswk-swf (DE-588)4113937-9 Hochschulschrift gnd-content Hitzeschock-Proteine (DE-588)4255487-1 s Biochemie (DE-588)4006777-4 s NMR-Spektroskopie (DE-588)4075421-2 s DE-604 Erscheint auch als Online-Ausgabe urn:nbn:de:bvb:91-diss-20120612-1099102-0-9 http://mediatum.ub.tum.de/node?id=1099102 Verlag kostenfrei Volltext https://nbn-resolving.org/urn:nbn:de:bvb:91-diss-20120612-1099102-0-9 Resolving-System DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=025862824&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Lagleder, Stephan Biochemical and NMR spectroscopic investigations on the Hsp90 chaperone system Hitzeschock-Proteine (DE-588)4255487-1 gnd Biochemie (DE-588)4006777-4 gnd NMR-Spektroskopie (DE-588)4075421-2 gnd |
| subject_GND | (DE-588)4255487-1 (DE-588)4006777-4 (DE-588)4075421-2 (DE-588)4113937-9 |
| title | Biochemical and NMR spectroscopic investigations on the Hsp90 chaperone system |
| title_auth | Biochemical and NMR spectroscopic investigations on the Hsp90 chaperone system |
| title_exact_search | Biochemical and NMR spectroscopic investigations on the Hsp90 chaperone system |
| title_full | Biochemical and NMR spectroscopic investigations on the Hsp90 chaperone system Stephan Lagleder |
| title_fullStr | Biochemical and NMR spectroscopic investigations on the Hsp90 chaperone system Stephan Lagleder |
| title_full_unstemmed | Biochemical and NMR spectroscopic investigations on the Hsp90 chaperone system Stephan Lagleder |
| title_short | Biochemical and NMR spectroscopic investigations on the Hsp90 chaperone system |
| title_sort | biochemical and nmr spectroscopic investigations on the hsp90 chaperone system |
| topic | Hitzeschock-Proteine (DE-588)4255487-1 gnd Biochemie (DE-588)4006777-4 gnd NMR-Spektroskopie (DE-588)4075421-2 gnd |
| topic_facet | Hitzeschock-Proteine Biochemie NMR-Spektroskopie Hochschulschrift |
| url | http://mediatum.ub.tum.de/node?id=1099102 https://nbn-resolving.org/urn:nbn:de:bvb:91-diss-20120612-1099102-0-9 http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=025862824&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
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