Membrane biogenesis and protein targeting:
Gespeichert in:
| Format: | Buch |
|---|---|
| Sprache: | English |
| Veröffentlicht: |
Amsterdam [u.a.]
Elsevier
1992
|
| Schriftenreihe: | New comprehensive biochemistry
22 |
| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XX, 343 S. Ill., graph. Darst. |
| ISBN: | 0444896384 |
Internformat
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| 245 | 1 | 0 | |a Membrane biogenesis and protein targeting |c ed. Walter Neupert ... |
| 264 | 1 | |a Amsterdam [u.a.] |b Elsevier |c 1992 | |
| 300 | |a XX, 343 S. |b Ill., graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
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| 490 | 1 | |a New comprehensive biochemistry |v 22 | |
| 650 | 4 | |a Biogenesis | |
| 650 | 4 | |a Biological Transport | |
| 650 | 4 | |a Membrane Proteins |x metabolism | |
| 650 | 4 | |a Membrane proteins |x Physiological transport | |
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| adam_text | IMAGE 1
XI
CONTENTS
LIST OF CONTRIBUTORS V
PART A BACTERIA
CHAPTER I. WHERE ARE WE IN THE EXPLORATION OF ESCHERICHIA COLI
TRANSLOCATION PATHWAYS?
BILL WICKNER 3
1. PROTEIN TRANSLOCATION PATHWAYS 4
2. OPEN QUESTIONS 6
REFERENCES 7
CHAPTER 2. COMPONENTS INVOLVED IN BACTERIAL PROTEIN TRANSLOCATION CHRIS
HARRIS AND PHANG C. TAI 9
1. INTRODUCTION 9
2. THE MINIMAL LENGTH OF A PROKARYOTIC SIGNAL PEPTIDE 10
3. THE N(M) ELEMENT: AN EXPORT REQUIREMENT FOR LOW BASICITY AS WELL AS
LOW POLARITY 12
4. IS SECY/PRLA ESSENTIAL FOR PROTEIN TRANSLOCATION? 14
5. IN VITRO SUPPRESSION OF DEFECTIVE SIGNAL PEPTIDES 15
6. ROLES OF SECD AND SECF IN PROTEIN TRANSLOCATION 16
7. AN INHIBITOR OF PROTEIN TRANSLOCATION 17
8. PERSPECTIVE 18
REFERENCES 18
CHAPTER 3. MOLECULAR CHARACTERIZATION OF SEC PROTEINS COMPRISING THE
PROTEIN SECRETORY MACHINERY OF ESCHERICHIA COLI SHOJI MIZUSHIMA, HAJIME
TOKUDA AND SHIN-ICHI MATSUYAMA 21
1. INTRODUCTION 21
2. OVERPRODUCTION OF SEC PROTEINS 22
3. PURIFICATION OF SEC PROTEINS 23
4. ESTIMATION OF THE NUMBERS OF SEC PROTEINS AND OF THE SECRETORY
MACHINERY IN ONE E. COLI CELL 24
5. FUNCTIONS OF SECA IN PROTEIN TRANSLOCATION 25
6. FUNCTIONS OF SECE AND SECY 27
7. FUNCTIONS OF SECD AND SECF 28
8. DISCUSSION 28
REFERENCES 30
IMAGE 2
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CHAPTER 4. DISTINCT STEPS IN THE INSERTION PATHWAY OF BACTERIOPHAGE COAT
PROTEINS ANDREAS KUHN AND DOROTHEE TROSCHEL 33
1. INTRODUCTION 33
2. RESULTS AND DISCUSSION 34
2.1. PF3 COAT PROTEIN REQUIRES NO LEADER SEQUENCE FOR MEMBRANE INSERTION
. . 34 2.2. HYBRID COAT PROTEINS OF M13 AND PF3 35
2.3. M L3 PROCOAT PROTEIN FIRST BINDS ELECTROSTATICALLY TO THE MEMBRANE
SURFACE 36 2.4. BOTH HYDROPHOBIC REGIONS ARE REQUIRED FOR THE
PARTITIONING OF THE M13 PROCOAT PROTEIN INTO THE MEMBRANE 38
2.5. TRANSLOCATION OF THE NEGATIVELY CHARGED PERIPLASMIC REGION OF THE
ML 3 PROCOAT PROTEIN IS NOT PRIMARILY AN ELECTROPHORETIC EVENT 39
2.6. M L3 PROCOAT PROTEIN AS A MODEL SUBSTRATE FOR LEADER PEPTIDASE 41
2.7. FROM MEMBRANE TO PHAGE 42
2.8. THE SEC-INDEPENDENT INSERTION PATHWAY IS LIMITED TO SIMPLE MEMBRANE
TRANSLOCATION DOMAINS 42
3. CONCLUSIONS 45
REFERENCES 46
CHAPTER 5. STEPS IN THE ASSEMBLY OF A CYTOPLASMIC MEMBRANE PROTEIN: THE
MALF COMPONENT OF THE MALTOSE TRANSPORT COMPLEX BETH TRAXLER AND JON
BECKWITH 49
1. INTRODUCTION 49
1.1. ISSUES IN THE STUDY OF MEMBRANE PROTEIN ASSEMBLY AND STRUCTURE . .
.. 49
1.2. THE MALF PROTEIN AS A MODEL SYSTEM 51
1.3. THE MECHANISM OF INSERTION INTO THE MEMBRANE OF MALF 52
2. THE NATURE OF TOPOGENIC SIGNALS IN MALF 53
3. KINETICS OF ASSEMBLY OF MALF IN THE CYTOPLASMIC MEMBRANE 56
4. ASSEMBLY OF MALF INTO THE QUATERNARY MALF-MALG-MALK STRUCTURE 57
5. SUMMARY 59
REFERENCES 60
CHAPTER 6. STRUCTURAL CHARACTERISTICS OF PRESECRETORY PROTEINS: THEIR
IMPLICATION AS TO TRANSLOCATION COMPETENCY SHOJI MIZUSHIMA, KATSUKO
TANI, CHINAMI HIKITA AND MASASHI KATO . . .. 63
1. INTRODUCTION 64
2. AMINO TERMINAL POSITIVE CHARGE OF THE SIGNAL PEPTIDE 64
3. CENTRAL HYDROPHOBIC STRETCH OF THE SIGNAL PEPTIDE 65
4. FUNCTION OF THE POSITIVE CHARGE CAN BE COMPENSATED FOR BY A LONGER
HYDROPHOBIC STRETCH 67
5. CARBOXYL TERMINAL REGION OF THE SIGNAL PEPTIDE INCLUDING THE CLEAVAGE
SITE . .. 68 6. ROLES OF CHARGED AMINO ACID RESIDUES IN THE MATURE
DOMAIN IN PROTEIN TRANSLOCATION 70
7. CHEMICAL STRUCTURE OF THE MATURE DOMAIN TOLERATED BY THE SECRETORY
MACHINERY 72 REFERENCES 73
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CHAPTER 7. SEQUENCE DETERMINANTS OF MEMBRANE PROTEIN TOPOLOGY
GUNNAR VON HEIJNE 75
1. INTRODUCTION 75
2. RESULTS 76
2.1. SIGNALS AND TOPOLOGIES 76
2.2. THE POSITIVE INSIDE-RULE 78
2.3. POSITIVELY CHARGED RESIDUES CONTROL MEMBRANE PROTEIN TOPOLOGY . .
.. 78
2.4. A MEMBRANE PROTEIN WITH PH-DEPENDENT TOPOLOGY 80
2.5. POSITION-SPECIFIC CHARGE-PAIRING CAN AFFECT THE TOPOLOGY 80
2.6. SEC-DEPENDENT VERSUS SEC-INDEPENDENT ASSEMBLY 81
3. DISCUSSION 82
REFERENCES 83
CHAPTER 8. LIPID INVOLVEMENT IN PROTEIN TRANSLOCATION B. DE KRUIJFF, E.
BREUKINK, R.A. DEMEL, R. VAN T HOF, H.H.J. DE JONGH, W. JORDI, R.C.A.
KELLER, J.A. KILLIAN, A.I.P.M. DE KROON, R. KUSTERS AND M. PILON 85
1. INTRODUCTION 85
2. RESULTS AND DISCUSSION 86
2.1. PROKARYOTIC PROTEIN SECRETION 86
2.2. MITOCHONDRIAL PROTEIN IMPORT 91
2.3. CHLOROPLAST PROTEIN IMPORT 97
3. CONCLUDING REMARKS 99
REFERENCES 99
PART B ENDOPLASMIC RETICULUM
CHAPTER 9. MEMBRANE PROTEIN INSERTION INTO THE ENDOPLASMIC RETICULUM:
SIGNALS, MACHINERY AND MECHANISMS STEPHEN HIGH AND BERNHARD BOBBER STEIN
105
1. INTRODUCTION 105
2. TYPES OF MEMBRANE PROTEINS AND THEIR TOPOLOGICAL SIGNALS 105
2.1. PROTEINS WITH UNCLEAVED SIGNAL SEQUENCES 106
2.2. PROTEINS WITH CLEAVABLE SIGNAL SEQUENCES 107
2.3. THE LOOP MODEL FOR PROTEIN INSERTION INTO THE MEMBRANE 108
2.4. BIOSYNTHESIS OF MULTIPLE SPANNING MEMBRANE PROTEINS 109
3. COMPONENTS INVOLVED IN THE INSERTION OF PROTEINS INTO THE ER MEMBRANE
. .. I LL 3.1. TARGETING I LL
3.2. MEMBRANE INSERTION I LL
3.3. GTP REQUIREMENT 114
4. DISCUSSION 115
REFERENCES 117
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CHAPTER 10. TRANSLOCATION OF PROTEINS THROUGH THE ENDOPLASMIC RETICULUM
MEMBRANE: INVESTIGATION OF THEIR MOLECULAR ENVIRONMENT BY CROSS-LINKING
ENNO HARTMANN AND TOM A. RAPOPORT 119
1. INTRODUCTION 119
2. RESULTS 120
2.1. EXPERIMENTAL STRATEGIES 120
2.2. THE SSR-COMPLEX 121
2.3. THE TRAM PROTEIN 122
2.4. OTHER GLYCOPROTEINS 123
2.5. UNGLYCOSYLATED PROTEINS 123
2.6. THE SEC PROTEINS OF YEAST MICROSOMES 124
3. DISCUSSION 124
REFERENCES 126
CHAPTER 11. THE ROLE OF GTP IN PROTEIN TARGETING TO THE ENDOPLASMIC
RETICULUM
STEPHEN C. OGG, JODI M. NUNNARI, JOSHUA D. MILLER AND PETER WALTER . ..
129
REFERENCES 135
CHAPTER 12. CONSECUTIVE STEPS OF NUCLEOSIDE TRIPHOSPHATE HYDROLYSIS ARE
DRIVING TRANSPORT OF PRECURSOR PROTEINS INTO THE ENDOPLASMIC RETICULUM
PETER KLAPPA, GIINTER MUTTER, GABRIEL SCHLENSTEDT, HANS WIECH AND
RICHARD ZIMMERMANN 137
1. INTRODUCTION 137
2. RESULTS 138
2.1. RIBONUCLEOPARTICLES VERSUS MOLECULAR CHAPERONES 139
2.2. TRANSLOCASE 141
3. DISCUSSION 143
3.1. COMPONENTS INVOLVED IN PROTEIN TRANSPORT INTO YEAST ENDOPLASMIC
RETICULUM 143 3.2. MODEL FOR RIBONUCLEOPARTICLE-INDEPENDENT TRANSPORT
143
3.3. OPEN QUESTIONS 144
REFERENCES 145
PART C VACUOLES
CHAPTER 13. MECHANISM AND REGULATION OF IMPORT AND DEGRADATION OF
CYTOSOLIC PROTEINS IN THE LYSOSOME/VACUOLE HUI-LING CHIANG AND RANDY
SCHEKMAN 149
1. INTRODUCTION 150
2. INTRACELLULAR PROTEIN DEGRADATION IN MAMMALIAN LYSOSOMES 151
2.1. MICROAUTOPHAGY 151
2.2. MACROAUTOPHAGY 152
2.3. LYSOSOMAL PROTEIN DEGRADATION IN CULTURED FIBROBLASTS 153
3. PROTEIN DEGRADATION IN THE YEAST VACUOLE 156
IMAGE 5
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3.1. CATABOLITE INACTIVATION 156
3.2. VACUOLAR DEGRADATION OF FBPASE 158
3.3. MECHANISM OF FBPASE DEGRADATION 159
3.4. COVALENT MODIFICATIONS AND FBPASE DEGRADATION 160
3.4.1. PHOSPHORYLATION 160
3.4.2. UBIQUITINATION 161
REFERENCES 162
CHAPTER 14. THE SORTING OF SOLUBLE AND INTEGRAL MEMBRANE PROTEINS TO THE
YEAST VACUOLE CHRISTOPHER K. RAYMOND, CAROL A. VATER, STEVEN NOTHWEHR,
CHRISTOPHER J.
ROBERTS AND TOM H. STEVENS 165
1. INTRODUCTION 165
2. RESULTS 167
2.1. NO SINGLE DOMAIN OF THE VACUOLAR INTEGRAL MEMBRANE PROTEIN DPAP B
IS REQUIRED FOR VACUOLAR DELIVERY 167
2.2. THE CYTOPLASMIC DOMAIN OF DPAP A IS NECESSARY AND SUFFICIENT FOR
ITS LOCALIZATION TO A LATE GOLGI COMPARTMENT 169
2.3. VPSLP, WHICH IS REQUIRED FOR THE SORTING OF SOLUBLE VACUOLAR
GLYCOPROTEINS, SHARES EXTENSIVE SIMILARITY WITH A SUBFAMILY OF
GTP-BINDING PROTEINS . . 170 2.4. VPSLP BINDS AND HYDROLYZES GTP 172
2.5. MUTATIONAL ANALYSIS SUGGESTS THAT VPSLP IS COMPOSED OF TWO
FUNCTIONALLY DISTINCT DOMAINS 173
3. DISCUSSION 177
3.1. TARGETING OF INTEGRAL MEMBRANE PROTEINS IN THE SECRETORY PATHWAY OF
SACCHAROMYCES CEREVISIAE 177
3.2. VPSLP, WHICH IS A GTPASE REQUIRED FOR THE SORTING OF SOLUBLE
VACUOLAR PROTEINS, IS COMPOSED OF TWO FUNCTIONALLY DISTINCT DOMAINS 179
REFERENCES 181
PART D PEROXISOMES
CHAPTER 15. DEFINING COMPONENTS REQUIRED FOR PEROXISOME ASSEMBLY IN
SACCHAROMYCES CEREVISIAE JORG HOHFELD, DAPHNE MERTENS, FRANZISKA F.
WIEBEL AND WOLF-H. KUNAU . . 185
1. INTRODUCTION 185
2. RESULTS 187
2.1. PEROXISOMAL MUTANTS OF SACCHAROMYCES CEREVISIAE 187
2.1.1. DEFECTS IN PEROXISOME FORMATION (TYPE I PAS MUTANTS: PASL, PAS2,
PAS3, PAS5) 189
2.1.2. DEFECTS IN PEROXISOME PROLIFERATION (TYPE II PAS MUTANTS: PAS4
AND PAS6) 191
2.1.3. DEFECTS IN IMPORT OF 3-OXOACYL-COA THIOLASE (TYPE III PAS MUTANT:
PAS7) 191
2.2. CLONING OF PEROXISOMAL GENES 191
2.3. SEQUENCE ANALYSIS 192
IMAGE 6
XVI
2.3.1. PAS1 192
2.3.2. PAS2 194
2.3.3. PAS4 194
2.4. IDENTIFICATION AND CHARACTERIZATION OF THE GENE PRODUCTS 195
2.5. ANALYSIS OF THE FUNCTION OF THE CLONED GENES FOR PEROXISOME
BIOGENESIS . 196 2.5.1. OVEREXPRESSION OF PAS4 196
2.5.2. SITE DIRECTED MUTAGENESIS 197
2.5.3. CONDITIONAL PEROXISOMAL MUTANTS 197
2.6. FUSION PROTEINS AS TOOLS FOR FURTHER INVESTIGATIONS 199
3. DISCUSSION 200
3.1. PEROXISOMAL MUTANTS AS A TOOL TO DISSECT PEROXISOME BIOGENESIS . .
.. 200
3.2. DO PEROXISOMAL PRESTRUCTURES EXIST IN TYPE I PAS MUTANTS? 202
3.3. ARE TYPE I PAS MUTANTS PEROXISOMAL IMPORT MUTANTS? 203
3.4. DO MORE PEROXISOMAL IMPORT ROUTES EXIST OTHER THAN THE SKL-MEDIATED
PATHWAY? 203
3.5. ARE TYPE II PAS MUTANTS AFFECTED IN PEROXISOME PROLIFERATION? 204
4. CONCLUSIONS 205
REFERENCES 205
CHAPTER 16. STRUCTURE AND ASSEMBLY OF PEROXISOMAL MEMBRANE PROTEINS JOEL
M. GOODMAN, LISA J. GARRARD AND MARK T. MCCAMMON 209
1. INTRODUCTION 210
2. RESULTS 210
2.1. ASSEMBLY OF PEROXISOMAL PROTEINS 212
2.2. PROLIFERATION OF PEROXISOMAL COMPONENTS 213
2.3. STRUCTURE AND COMPOSITION OF PEROXISOMAL MEMBRANES 213
2.4. CLONING OF GENES ENCODING MEMBRANE PROTEINS 214
2.5. EXPRESSION AND SORTING OF PMP47 215
3. DISCUSSION 217
REFERENCES 219
CHAPTER 17. MECHANISMS OF TRANSPORT OF PROTEINS INTO MICROBODIES SURESH
SUBRAMANI ; 221
1. INTRODUCTION 221
2. A C-TERMINAL TRIPEPTIDE IS A MAJOR TARGETING SIGNAL FOR PROTEINS OF
THE MICROBODY MATRIX 223
3. CERTAIN VARIANTS OF THE SKL TRIPEPTIDE CAN ALSO FUNCTION AS PTS 224
4. PEROXISOMAL PROTEIN TRANSPORT IN MICROINJECTED MAMMALIAN CELLS 224
5. IMPORT DEFICIENCY IN FIBROBLAST CELLS FROM ZELLWEGER S SYNDROME
PATIENTS. . . . 225 6. AN AMINO-TERMINAL PTS RESIDES IN THE CLEAVED
LEADER PEPTIDES OF THE PEROXISOMAL THIOLASES 226
7. SELECTIVE IMPORT DEFICIENCY IN ZELLWEGER CELLS 226
8. TRANSPORT OF MEMBRANE PROTEINS INTO PEROXISOMES 227
9. SUMMARY 227
REFERENCES 227
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CHAPTER 18. LESSONS FOR PEROXISOME BIOGENESIS FROM FLUORESCENCE ANALYSES
OF
ZELLWEGER SYNDROME FIBROBLASTS PAUL B. LAZAROW, HUGO W. MOSER AND MANUEL
J. SANTOS 231
1. INTRODUCTION 231
2. RESULTS 232
3. DISCUSSION 233
3.1. PEROXISOME MEMBRANES ARE ALWAYS PRESENT: PERHAPS THEY ARE REQUIRED
FOR VIABILITY 233
3.2. THE PEROXISOME MEMBRANES ARE NEARLY EMPTY GHOSTS: THESE ARE
PEROXISOME IMPORT (PIM) MUTATIONS 234
3.3. PEROXISOME MEMBRANE ASSEMBLY HAS FEWER REQUIREMENTS, OR DIFFERENT
REQUIREMENTS, FROM THE PACKAGING OF PEROXISOME MATRIX PROTEINS 234 3.4.
EMPTY PEROXISOME MEMBRANE GHOSTS DIVIDE 235
3.5. GENETIC COMPLEMENTATION FOR PEROXISOME ASSEMBLY IS FORMALLY
DEMONSTRATED 235
3.6. PRELIMINARY PARTIAL CORRELATION OF GENOTYPE AND PHENOTYPE 236
3.7. FUTURE DIRECTIONS 236
REFERENCES 236
PART E MITOCHONDRIA
CHAPTER 19. THE MITOCHONDRIA! PROTEIN IMPORT MACHINERY OF SACCHAROMYCES
CEREVISIAE VICTORIA HINES 241
1. INTRODUCTION 241
2. COMPONENTS OF THE IMPORT MACHINERY 242
2.1. IMPORT RECEPTORS 242
2.2. THE PROTEIN TRANSLOCATION CHANNEL 245
2.3. REFOLDING AND PROCESSING PROTEINS 245
3. THE MECHANISM OF PROTEIN IMPORT 246
3.1. ENERGY REQUIREMENTS 246
3.2. CONTACT SITES 247
3.3. PROTEIN SORTING 248
4. OUTLOOK 250
REFERENCES 250
CHAPTER 20. PROTEIN INSERTION INTO MITOCHONDRIAL OUTER AND INNER
MEMBRANES VIA THE STOP-TRANSFER SORTING PATHWAY GORDON C. SHORE, DOUGLAS
G. MILLAR AND JIAN-MING LI 253
1. INTRODUCTION 254
2. RESULTS AND DISCUSSION 256
2.1. MITOCHONDRIAL TOPOGENIC SEQUENCES AND STOP-TRANSFER SORTING 256
2.2. THE OMM SIGNAL-ANCHOR SEQUENCE 256
2.3. STOP-TRANSFER SORTING TO THE INNER MEMBRANE 257
IMAGE 8
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2.4. POLYTOPIC PROTEINS 259
2.5. DEFAULT SORTING 259
3. CONCLUSIONS 261
REFERENCES 262
CHAPTER 21. GENERAL AND EXCEPTIONAL PATHWAYS OF PROTEIN IMPORT INTO
SUB-MITOCHONDRIAL COMPARTMENTS ROLAND LILL, CHRISTOPH HERGERSBERG,
HELMUT SCHNEIDER, THOMAS SOLLNER, ROSEMARY STUART AND WALTER NEUPERT 265
1. THE GENERAL PATHWAYS FOR PROTEIN IMPORT INTO SUB-MITOCHONDRIAL
COMPARTMENTS. 265 2. EXCEPTIONAL PATHWAYS OF PROTEIN IMPORT 268
3. MOM 19 IS IMPORTED INTO THE OM WITHOUT THE AID OF SURFACE RECEPTORS .
. .. 269
4. CYTOCHROME C HEME LYASE IS IMPORTED DIRECTLY THROUGH THE OM VIA A
NON-CONSERVATIVE SORTING PATHWAY 271
5. PERSPECTIVES 274
REFERENCES 275
PART F CHLOROPLASTS
CHAPTER 22. TARGETING OF PROTEINS INTO AND ACROSS THE CHLOROPLASTIC
ENVELOPE H.-M. LI, S.E. PERRY AND K. KEEGSTRA 279
1. INTRODUCTION 280
2. TRANSPORT ACROSS THE ENVELOPE MEMBRANES 281
2.1. BINDING OF PRECURSORS TO THE CHLOROPLASTIC SURFACE 281
2.2. TRANSLOCATION OF PRECURSOR ACROSS THE ENVELOPE MEMBRANES 283
3. TARGETING OF PROTEINS INTO THE ENVELOPE MEMBRANES 284
3.1. TARGETING TO THE OUTER ENVELOPE MEMBRANE 284
3.2. TARGETING TO THE INNER ENVELOPE MEMBRANE 286
4. SUMMARY AND FUTURE PROSPECTS 287
REFERENCES 287
CHAPTER 23. TRANSPORT OF PROTEINS INTO THE THYLAKOIDS OF HIGHER PLANT
CHLOROPLASTS COLIN ROBINSON 289
1. INTRODUCTION 289
2. RESULTS 291
2.1. DEVELOPMENT OF AN IN VITRO ASSAY FOR THE IMPORT OF PROTEINS BY
ISOLATED THYLAKOIDS 291
2.2. ENERGY REQUIREMENTS FOR THE IMPORT OF PROTEINS INTO ISOLATED
THYLAKOIDS . 292 2.3. EVENTS IN THE STROMA 292
2.4. MATURATION OF IMPORTED THYLAKOID LUMEN PROTEINS 295
3. DISCUSSION 295
REFERENCES 296
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CHAPTER 24. COMPARISON OF TWO DIFFERENT PROTEIN TRANSLOCATION MECHANISMS
INTO CHLOROPLASTS JIIRGEN SOIL, HEIKE ALEFSEN, BIRGIT BOCKLER, BIRGIT
KERBER, MICHAEL SALOMON
AND KARIN WAEGEMANN 299
1. INTRODUCTION 299
2. RESULTS AND DISCUSSION 299
2.1. IMPORT CHARACTERISTICS OF PSSU AND OEP 7 299
2.2. SPECIFICITY AND MECHANISM OF OEP 7 INSERTION 301
REFERENCES 306
PART G CHAPERONES
CHAPTER 25. DNAJ HOMOLOGS AND PROTEIN TRANSPORT TAKAO KURIHARA AND
PAMELA A. SILVER 309
1. INTRODUCTION 309
1.1. STIMULATION OF PROTEIN TRANSPORT BY HSP70S AND ADDITIONAL FACTORS .
. . 309 1.2. E. COLI DNAJ AND GRPE FUNCTION WITH AND REGULATE BACTERIAL
HSP70 (DNAK) 310 1.2.1. BACTERIOPHAGE 1 AND PI REPLICATION AND PROTEIN
COMPLEX DISASSEMBLY 311
1.2.2. REFOLDING OF THERMALLY INACTIVATED ACI857 REPRESSOR 312
1.2.3. PROTEOLYSIS OF PUROMYCIN-GENERATED POLYPEPTIDE FRAGMENTS . . 312
1.2.4. STIMULATION OF DNAK ATPASE ACTIVITY BY DNAJ AND GRPE . . 313 2.
RESULTS 313
2.1. DNAJ HOMOLOGS 313
2.1.1. BACTERIAL DNAJ HOMOLOGS 316
2.1.2. DNAJ HOMOLOGS IN THE YEAST SACCHAROMYCES CEREVISIAE . . .. 316
2.1.3. SCJ1 316
2.1.4. YDJ1/MAS5 317
2.1.5. SIS1 318
2.1.6. NPL1/SEC63 319
2.2. THE J-REGION 321
2.2.1. THE NPL1/SEC63 J-REGION: LOCALIZATION TO THE ER LUMEN . . 321
2.2.2. GENETIC EVIDENCE FOR J-REGION ROLE IN KAR2 INTERACTION AND ER
TRANSLOCATION 323
3. DISCUSSION 323
3.1. MODEL FOR NPL 1/SEC63 FUNCTION 323
3.2. DNAJ HOMOLOGS, J-REGIONS AND PROTEIN TRANSPORT 324
REFERENCES 325
CHAPTER 26. CHAPERONIN-MEDIATED PROTEIN FOLDING ARTHUR L. HORWICH, SHARI
CAPLAN, JOSEPH S. WALL AND F.-ULRICH HARTL . .. 329
1. INTRODUCTION 329
2. IN VIVO ANALYSIS OF CHAPERONIN FUNCTION 330
3. ROLE OF HSP60 IN BIOGENESIS OF MITOCHONDRIAL-ENCODED PROTEINS 331
4. CHAPERONIN-MEDIATED FOLDING RECONSTITUTED IN VITRO 333
IMAGE 10
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5. MODELS FOR PHYSICAL INTERACTIONS OF COMPONENTS IN CHAPERONIN-MEDIATED
FOLDING 334 REFERENCES 337
INDEX 339
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| classification_tum | CHE 820f CHE 887f |
| ctrlnum | (OCoLC)26218211 (DE-599)BVBBV006495002 |
| dewey-full | 574.87/5 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 574 - [Unassigned] |
| dewey-raw | 574.87/5 |
| dewey-search | 574.87/5 |
| dewey-sort | 3574.87 15 |
| dewey-tens | 570 - Biology |
| discipline | Biologie Chemie |
| format | Book |
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| genre | (DE-588)4143413-4 Aufsatzsammlung gnd-content Targetanalyse gnd |
| genre_facet | Aufsatzsammlung Targetanalyse |
| id | DE-604.BV006495002 |
| illustrated | Illustrated |
| indexdate | 2024-07-09T16:47:09Z |
| institution | BVB |
| isbn | 0444896384 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-004130270 |
| oclc_num | 26218211 |
| open_access_boolean | |
| owner | DE-19 DE-BY-UBM DE-12 DE-355 DE-BY-UBR DE-703 DE-29 DE-83 DE-188 |
| owner_facet | DE-19 DE-BY-UBM DE-12 DE-355 DE-BY-UBR DE-703 DE-29 DE-83 DE-188 |
| physical | XX, 343 S. Ill., graph. Darst. |
| publishDate | 1992 |
| publishDateSearch | 1992 |
| publishDateSort | 1992 |
| publisher | Elsevier |
| record_format | marc |
| series | New comprehensive biochemistry |
| series2 | New comprehensive biochemistry |
| spelling | Membrane biogenesis and protein targeting ed. Walter Neupert ... Amsterdam [u.a.] Elsevier 1992 XX, 343 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier New comprehensive biochemistry 22 Biogenesis Biological Transport Membrane Proteins metabolism Membrane proteins Physiological transport Membrantransport (DE-588)4038575-9 gnd rswk-swf Membranproteine (DE-588)4130026-9 gnd rswk-swf Biomembran (DE-588)4006884-5 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Targetanalyse gnd rswk-swf Membranproteine (DE-588)4130026-9 s Targetanalyse f DE-604 Membrantransport (DE-588)4038575-9 s Biomembran (DE-588)4006884-5 s Neupert, Walter 1939-2019 Sonstige (DE-588)104537217X oth New comprehensive biochemistry 22 (DE-604)BV000003914 22 SWB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=004130270&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Membrane biogenesis and protein targeting New comprehensive biochemistry Biogenesis Biological Transport Membrane Proteins metabolism Membrane proteins Physiological transport Membrantransport (DE-588)4038575-9 gnd Membranproteine (DE-588)4130026-9 gnd Biomembran (DE-588)4006884-5 gnd |
| subject_GND | (DE-588)4038575-9 (DE-588)4130026-9 (DE-588)4006884-5 (DE-588)4143413-4 |
| title | Membrane biogenesis and protein targeting |
| title_auth | Membrane biogenesis and protein targeting |
| title_exact_search | Membrane biogenesis and protein targeting |
| title_full | Membrane biogenesis and protein targeting ed. Walter Neupert ... |
| title_fullStr | Membrane biogenesis and protein targeting ed. Walter Neupert ... |
| title_full_unstemmed | Membrane biogenesis and protein targeting ed. Walter Neupert ... |
| title_short | Membrane biogenesis and protein targeting |
| title_sort | membrane biogenesis and protein targeting |
| topic | Biogenesis Biological Transport Membrane Proteins metabolism Membrane proteins Physiological transport Membrantransport (DE-588)4038575-9 gnd Membranproteine (DE-588)4130026-9 gnd Biomembran (DE-588)4006884-5 gnd |
| topic_facet | Biogenesis Biological Transport Membrane Proteins metabolism Membrane proteins Physiological transport Membrantransport Membranproteine Biomembran Aufsatzsammlung Targetanalyse |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=004130270&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| volume_link | (DE-604)BV000003914 |
| work_keys_str_mv | AT neupertwalter membranebiogenesisandproteintargeting |