Ubiquitin:
Saved in:
| Format: | Book |
|---|---|
| Language: | English |
| Published: |
New York u.a.
Plenum Pr.
1988
|
| Subjects: | |
| Online Access: | Inhaltsverzeichnis |
| Physical Description: | XVIII, 346 S. |
| ISBN: | 0306428504 |
Staff View
MARC
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Record in the Search Index
| _version_ | 1804115736769069056 |
|---|---|
| adam_text | IMAGE 1
UBIQUITIN
EDITED BY
MARTIN RECHSTEINER UNIVERSITY OF UTAH SCHOOL OF MEDICINE SALT LAKE CITY,
UTAH
PLENUM PRESS * NEW YORK AND LONDON
IMAGE 2
CONTENTS
I N T R O D U C T I ON . ..
MARTIN RECHSTEINER
CHAPTER 1
PURIFICATION AND STRUCTURAL PROPERTIES OF UBIQUITIN
KEITH D. WILKINSON
1. INTRODUCTION 5
2. PURIFICATION OF UBIQUITIN 6
2.1. ASSAYS FOR UBIQUITIN 6
2.2. TISSUE SOURCE 9
2.3. PURIFICATION PROCEDURE 11
3. PHYSICAL CHARACTERISTICS OF UBIQUITIN 13
3.1. AMINO ACID SEQUENCE 13
3.2. CRYSTAL STRUCTURE 14
3.3. SPECTROSCOPIC PROPERTIES OF THE NATIVE AND ALCOHOL-INDUCED
CONFORMATIONS 16
3.4. DIGESTION BY PROTEASES 21
3.5. HYDRODYNAMIC PROPERTIES 22
3.6. BINDING AND CATALYTIC ACTIVITIES OF UBIQUITIN . .. 22
XI
IMAGE 3
XII CONTENTS
4. STRUCTURE-FUNCTION RELATIONS 23
4.1. NATURAL VARIANT SEQUENCES 25
4.2. CHEMICALLY MODIFIED UBIQUITIN 25
4.3. CONCLUSIONS 28
5. FUTURE DIRECTIONS OF STRUCTURAL CHEMISTRY 30
5.1. SITE-DIRECTED MUTAGENESIS 30
5.2. CARBOXYL-TERMINAL DERIVATIVES OF UBIQUITIN . . .. 31
5.3. APPROACHES TO DEFINING OTHER FUNCTIONS . . .. 33
6. CONCLUDING REMARKS 34
REFERENCES 35
CHAPTER 2
MOLECULAR GENETICS OF THE UBIQUITIN SYSTEM
DANIEL FINLEY, ENGIN OZKAYNAK, STEFAN JENTSCH, JOHN P. MCGRATH, BONNIE
BARTEL, MICHAEL PAZIN, ROBERT M. SNAPKA, AND ALEXANDER VARSHAVSKY
1. INTRODUCTION AND SUMMARY 39
2. CONDITIONAL UBIQUITINATION IN A MAMMALIAN CELL CYCLE MUTANT 41
2.1. TEMPERATURE SENSITIVITY OF UBIQUITIN-ACTIVATING ENZYME FROM TS85
CELLS 41
2.2. TEMPERATURE SENSITIVITY OF SELECTIVE PROTEIN DEGRADATION IN TS85
CELLS 42
2.3. PROTEINS INDUCED IN TS85 CELLS AT NONPERMISSIVE TEMPERATURE 47
2.4. OTHER PHENOTYPES OF TS85 CELLS 50
3. THE UBIQUITIN SYSTEM OF SACCHAROMYCES CEREVISIAE . .. 52
3.1. THE YEAST UBIQUITIN GENES: A FAMILY OF NATURAL GENE FUSIONS 52
3.2. THE POLYUBIQUITIN GENE IS ESSENTIAL FOR STRESS RESISTANCE 56
3.3. ANALYSIS OF THE UBIQUITIN-HYBRID GENES 61
3.4. THE YEAST 0 UBIQUITIN-PROTEIN LIGASE SYSTEM . . .. 63
3.5. THE DNA REPAIR GENE RAD6 ENCODES A UBIQUITIN CARRIER PROTEIN 66
REFERENCES 70
IMAGE 4
CONTENTS XIII
CHAPTER 3
UBIQUITIN ACTIVATION AND LIGATION
CECILE M. PICKART
1. INTRODUCTION 77
2. SIGNIFICANCE OF UBIQUITIN-PROTEIN CONJUGATES IN UBIQUITIN-DEPENDENT
PROTEIN TURNOVER 78
2.1. HISTORICAL BACKGROUND 78
2.2. CONJUGATE FUNCTION 80
. 2.3. CONJUGATE STRUCTURE 82
3. ENZYMES OF UBIQUITIN ACTIVATION AND LIGATION 85
3.1. INTRODUCTION 85
3.2. INITIAL UBIQUITIN ACTIVATION: UBIQUITIN ACTIVATING ENZYME (EL) 87
3.3. UBIQUITIN TRANSTHIOLATION: UBIQUITIN CARRIER PROTEINS (E2S) 90
3.4. UBIQUITIN-PROTEIN LIGASE (E3): MECHANISM AND SIGNIFICANCE . 93
4. UNRESOLVED QUESTIONS 95
4.1. MECHANISTIC QUESTIONS 95
4.2. BIOLOGICAL QUESTIONS 96
REFERENCES 97
CHAPTER 4
UBIQUITIN/ATP-DEPENDENT PROTEASE
RONALD F. HOUGH, GREGORY W. PRATT, AND MARTIN RECHSTEINER
1. INTRODUCTION ~ 101
2. UBIQUITIN-LYSOZYME CONJUGATES 103
2.1. UNEXPECTED PROPERTIES 103
2.2. PURIFICATION AND SUBSTRATE CHARACTERISTICS 105
3. IDENTIFICATION OF AN ATP-DEPENDENT PROTEASE FROM RETICULOCYTES 108
4. PURIFICATION OF THE 26 S ATP-DEPENDENT PROTEASE AND A 20 S
MULTISUBUNIT PROTEASE FROM RETICULOCYTES . . .. 109
5. HIGH-MOLECULAR-WEIGHT CYTBSOLIC PROTEASES I LL
5.1. SUBUNIT STRUCTURE OF THE 26 S PROTEASE FROM RETICULOCYTES I LL
IMAGE 5
XIV CONTENTS
5.2. GENERAL FEATURES OF THE 20 S PROTEASE 112
5.3. ATP-DEPENDENT, STIMULATED, OR STABILIZED HIGH M R PROTEASES 119
5.4. STABILITY OF THE 26 S AND 20 S PROTEASES 121
5.5. SUBCELLULAR LOCATION OF 26 S AND 20 S PROTEASES . . 121 5.6.
STRUCTURAL MODELS FOR THE 26 S AND 20 S PROTEASES . . 122 6. OTHER
PROTEASES STIMULATED BY ATP 123
6.1. ADRENAL MITOCHONDRIAL ENZYME 123
6.2. ESCHERICHIA COLI MULTICOMPONENT PATHWAY . . .. 124
6.3. ESCHERICHIA COLI PROTEASE LA 125
7. THE ROLE OF ATP IN PROTEOLYSIS 125
8. NOMENCLATURE: MACROPAIN AND MEGAPAIN 126
9. MACROPAIN AND PROSOMES 127
10. ALTERNATE PROTEOLYTIC PATHWAYS 127
11. CONCLUSION = 128
REFERENCES 128
CHAPTER 5
UBIQUITIN CARBOXYL-TERMINAL HYDROLASES
IRWIN A. ROSE
1. INTRODUCTION 135
2. NOMENCLATURE 136
3. DISCOVERY OF UBIQUITIN HYDROLASES 136
4. NONPROTEIN LIGAND-UBIQUITIN HYDROLASES (ULH) . . .. 138
4.1. DISCOVERY 138
4.2. ASSAYS FOR UBIQUITIN CARBOXYL LIGAND HYDROLASES 139
4.3. PURIFICATION OF ULHS 140
4.4. SPECIFICITY AND MECHANISTIC STUDIES 140
5. UBAL SYNTHESIS AND EVIDENCE FOR OTHER UBAL-SENSITIVE HYDROLASES ~ 145
6. OTHER HYDROLASES WITH MOLECULAR WEIGHT ~30 KDA AND GREATER 147
7. UBIQUITIN-PROTEIN HYDROLASES 148
7.1. ASSAYS . 148
7.2. UBIQUITIN-HISTONE ISOPEPTIDASES 148
7.3. UBIQUITIN- E PROTEIN HYDROLASES OF RETICULOCYTES . . 149 7.4. ROLE
OF HYDROLASES IN THE UBIQUITIN/ATP-DEPENDENT PROTEOLYTIC PROCESS 150
IMAGE 6
CONTENTS XV
8. UBIQUITIN-PROTEIN PEPTIDASES ( U T H S) 152
9. CONCLUSION 153
REFERENCES 153
CHAPTER 6
UBIQUITINATED HISTONES AND CHRDMATIN
WILLIAM M. BONNER, CHRISTOPHER L. HATCH, AND ROY S. WU
1. INTRODUCTION 157
2. STRUCTURE 157
3. METABOLISM 161
3.1. CELL CYCLE STUDIES 163
3.2. OTHER METABOLIC STUDIES 164
4. HISTONE CONJUGATES AND TRANSCRIPTION 166
REFERENCES 168
CHAPTER 7
IMMUNOCHEMICAL PROBES OF UBIQUITIN POOL DYNAMICS
ARTHUR L. HAAS
1. INTRODUCTION 173
2. IMMUNOCHEMICAL METHODS 175
2.1. PREPARATION OF POLYCLONAL ANTIBODIES 175
2.2. SOLUTION PHASE QUANTITATION OF FREE UBIQUITIN . .. 177
2.3. SOLID PHASE QUANTITATION OF CONJUGATED UBIQUITIN . . 178 2.4.
VISUALIZATION OF UBIQUITIN CONJUGATES AFTER ELECTROPHORETIC TRANSFER 180
2.5. IMMUNOISOLATION OF UBIQUITIN CONJUGATES 181
2.6. IMMUNOHISTOCHEMICAL LOCALIZATION OF UBIQUITIN CONJUGATES 182
3. INTRACELLULAR UBIQUITIN POOLS 184
3.1. UBIQUITIN POOL SIZES IN CULTURED CELL LINES . . .. 184
3.2. UBIQUITIN POOLS WITHIN INTACT TISSUES 186
3.3. SUBCELLULAR LOCALIZATION OF UBIQUITIN CONJUGATES . . 191 3.4. THE
DYNAMICS OF UBIQUITIN POOLS 193
3.5. THE ROLE OF UBIQUITIN-PROTEIN LIGATION: A HYPOTHESIS 199
4. CONCLUSION 202
REFERENCES 202
IMAGE 7
XVI CONTENTS
CHAPTER 8
PROTEIN BREAKDOWN AND THE HEAT-SHOCK RESPONSE STEPHEN A. GOFF, RICHARD
VOELLMY, AND ALFRED L. GOLDBERG
1. INTRODUCTION 207
2. THE UBIQUITIN-INDEPENDENT PROTEOLYTIC SYSTEM IN ESCHERICHIA COLI 208
3. PROTEASE LA, THE ION GENE PRODUCT IN ESCHERICHIA COLI . . 210 4. THE
HEAT-SHOCK RESPONSE IN ESCHERICHIA COLI 211
5. ACTIVATION OF ION AND OTHER HEAT-SHOCK GENES BY ABNORMAL PROTEINS 214
6. PROTEOLYSIS AND REGULATION OF THE HEAT-SHOCK RESPONSE IN ESCHERICHIA
COLI 217
7. REGULATION OF HSP GENE EXPRESSION IN EUKARYOTIC CELLS * 221
8. HEAT-SHOCK PROTEINS IN EUKARYOTIC CELLS AND THEIR POSSIBLE FUNCTIONS
222
9. LINKS BETWEEN THE EUKARYOTIC HEAT-SHOCK SYSTEM AND PROTEIN
DEGRADATION 225
REFERENCES 228
CHAPTER 9
LYMPHOCYTE HOMING RECEPTORS, UBIQUITIN, AND CELL SURFACE PROTEINS
MARK SIEGELMAN AND IRVING L. WEISSMAN
1. INTRODUCTION 239
2. IN VITRO MODELS OF LYMPHOCYTE HOMING 242
2.1. INDEPENDENT HOMING RECEPTORS 243
2.2. IMMUNOLOGICAL IDENTIFICATION OF HOMING RECEPTORS _. 244
2.3. EXPRESSION OF THE MEL-14 EPITOPE DURING LYMPHOCYTE ACTIVATION 245
2.4. REGULATION OF LYMPHOCYTE HOMING RECEPTORS IN EARLY T AND B CELL
DEVELOPMENT 247
3. IS UBIQUITIN THE MEL-14 EPITOPE? 248
3.1. PURIFICATION OF THE CELL SURFACE GLYCOPROTEIN GP 90 MEL-14 249
3.2. A M I NO ACID S E Q U E N CE A N A L Y S IS OF G P 9 0 M E L - 4
. .. 250
3 . 3. G P 9 0 M E L 1 4 -A U B I Q U I T I N A T ED CELL SURFACE
P R O T E IN 253
3.4. N - L I N K ED G L Y C O S Y L A T I ON OF T HE M E L - 14 A N T I
G EN . . 255
IMAGE 8
CONTENTS XVLI
3.5. UBIQUITIN AS A UNIQUE CONFORMATIONAL DETERMINANT O F G P 9 0 M E L
14 256
4. A MODEL FOR THE HEV HOMING RECEPTOR 258
5. ADDITIONAL UBIQUITINATED CELL SURFACE PRODUCTS 259
6. POSSIBLE MECHANISMS FOR UBIQUITINATION OF CELL SURFACE PROTEINS 260
REFERENCES , 263
CHAPTER 10
ROLE OF TRANSFER RNA IN THE DEGRADATION OF SELECTIVE SUBSTRATES OF THE
UBIQUITIN- AND ATP-DEPENDENT PROTEOLYTIC SYSTEM
AARON CIECHANOVER
1. INTRODUCTION ^ 271
2. TRANSFER RNA AND THE DEGRADATION OF BOVINE SERUM ALBUMIN 272
3. REQUIREMENT OF TRNA FOR UBIQUITIN CONJUGATION . . .. 276
4. ROLE OF TRNA IN THE UBIQUITIN PATHWAY 279
5. CONCLUSION 283
REFERENCES 284
CHAPTER 11
THE N-END RULE OF SELECTIVE PROTEIN TURNOVER: MECHANISTIC ASPECTS AND
FUNCTIONAL IMPLICATIONS
ALEXANDER VARSHAVSKY, ANDREAS BACHMAIR, DANIEL FINLEY, DAVID GONDA, AND
INGRID WIINNING
1. INTRODUCTION 287
2. UBIQUITIN FUSION PROTEINS, AS IN VIVO PROTEOLYTIC SUBSTRATES 289
2.1. RAPID IN VIVO DEUBIQUITINATION OF A NASCENT UBIQUITIN-|3GAL FUSION
PROTEIN 289
2.2. THE IN VIVO HALF-LIFE OF PGAL IS A FUNCTION OF ITS AMINO-TERMINAL
RESIDUE 295
2.3. AMINO-TERMINAL LOCATION OF AN AMINO ACID IS ESSENTIAL FOR ITS
EFFECT ON PGAL HALF-LIFE 297
2.4. A LONG-LIVED CLEAVAGE PRODUCT OF PGAL FORMS DURING DECAY OF
SHORT-LIVED PGAL PROTEINS . . .. 298
2.5. UBIQUITIN-|3GAL IS SHORT-LIVED WHEN NOT DEUBIQUITINATED 298
IMAGE 9
XVIII CONTENTS
2.6. SHORT-LIVED PGAL PROTEINS ARE MULTIPLY UBIQUITINATED
IN VIVO 300
3. THE N-END RULE 300
3.1. AMINO-TERMINAL RESIDUES IN SEQUENCED INTRACELLULAR PROTEINS 300
3.2. AMINO-TERMINAL RESIDUES IN COMPARTMENTALIZED PROTEINS ARE LARGELY
OF THE DESTABILIZING CLASS . .. 301 3.3. THE N-END RULE PATHWAY 302
4. POSSIBLE ROLE OF THE N-END RULE PATHWAY IN THE TURNOVER OF LONG-LIVED
PROTEINS 303
5. FUNCTION OF POST-TRANSLATIONAL CONJUGATION OF AMINO ACIDS TO AMINO
TERMINI OF PROTEINS: PRIMARY AND SECONDARY DESTABILIZING AMINO ACIDS 304
6. AMINO TERMINAL VERSUS INTERIOR TARGETING IN SELECTIVE PROTEIN
TURNOVER 307
7. IN VITRO ANALYSIS OF THE N-END RULE PATHWAY 309
8. CURRENT PROBLEMS IN AMINO-TERMINAL TARGETING 311
9. ON THE FUNCTIONS OF UBIQUITINATION 317
10. CONCLUDING REMARKS 318
11. SUMMARY 319
REFERENCES 321
CHAPTER 12
SELECTIVITY OF UBIQUITIN-MEDIATED PROTEIN BREAKDOWN: CURRENT STATUS OF
OUR UNDERSTANDING
AVRAM HERSHKO
1. INTRODUCTION 325
2. MECHANISMS OF SELECTIVITY: QUESTIONS AND ASSUMPTIONS . . 326 3. ROLE
OF THE NH 2 : TERMINAL RESIDUE 326
4. OTHER POSSIBLE STRUCTURAL DETERMINANTS 327
4.1. PEST REGIONS 327
4.2. OXIDATION -. 328
4.3. PROTEIN UNFOLDING 328
5. SELECTIVITY OF E3 BINDING 329
5.1. SUBSTRATE FINDING SITE 329
5.2. HEAD AND BODY SUBSITES 330
6. CONCLUSION 330
REFERENCES 331
INDEX 333
|
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| genre_facet | Aufsatzsammlung |
| id | DE-604.BV001329460 |
| illustrated | Not Illustrated |
| indexdate | 2024-07-09T15:27:21Z |
| institution | BVB |
| isbn | 0306428504 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-000803529 |
| oclc_num | 17732253 |
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| physical | XVIII, 346 S. |
| publishDate | 1988 |
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| publisher | Plenum Pr. |
| record_format | marc |
| spelling | Ubiquitin ed. by Martin Rechsteiner New York u.a. Plenum Pr. 1988 XVIII, 346 S. txt rdacontent n rdamedia nc rdacarrier Protéines végétales ram Ubiquitin Ubiquitins Ubiquitin (DE-588)4314848-7 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Ubiquitin (DE-588)4314848-7 s DE-604 Rechsteiner, Martin Sonstige oth HEBIS Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=000803529&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Ubiquitin Protéines végétales ram Ubiquitin Ubiquitins Ubiquitin (DE-588)4314848-7 gnd |
| subject_GND | (DE-588)4314848-7 (DE-588)4143413-4 |
| title | Ubiquitin |
| title_auth | Ubiquitin |
| title_exact_search | Ubiquitin |
| title_full | Ubiquitin ed. by Martin Rechsteiner |
| title_fullStr | Ubiquitin ed. by Martin Rechsteiner |
| title_full_unstemmed | Ubiquitin ed. by Martin Rechsteiner |
| title_short | Ubiquitin |
| title_sort | ubiquitin |
| topic | Protéines végétales ram Ubiquitin Ubiquitins Ubiquitin (DE-588)4314848-7 gnd |
| topic_facet | Protéines végétales Ubiquitin Ubiquitins Aufsatzsammlung |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=000803529&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| work_keys_str_mv | AT rechsteinermartin ubiquitin |