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Langer, T., C. Lu, H. Echols, J. Flanagan, M. K. Hayer & F. U. Hartl, (1992) Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356: 683-689. Levinthal, C., (1968) Are there pathways for protein folding? Extrait du Journal de Chimie Physique 65: 44-45. Lewis, V. A., G. M. Hynes, D. Zheng, H. Saibil & K. Willison, (1992) T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol. Nature 358: 249-252. Lewthwaite, J., A. Skinner & B. Henderson, (1998) Are molecular chaperones microbial virulence factors? Trends Microbiol 6: 426-428. Lewthwaite, J. C., A. R. Coates, P. Tormay, M. Singh, P. Mascagni, S. Poole, M. Roberts, L. Sharp & B. Henderson, (2001) Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (Hsp 65) and contains a CD14- binding domain. Infect Immun 69: 7349-7355. Li, Y., X. Gao & L. Chen, (2009) GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side. J Biol Chem 284: 4324-4331. Li, Y., Z. Zheng, A. Ramsey & L. Chen, (2010) Analysis of peptides and proteins in their binding to GroEL. J Pept Sci. Lill, R., E. Crooke, B. Guthrie & W. Wickner, (1988) The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane. Cell 54: 1013-1018. Lin, C. Y., Y. S. Huang, C. H. Li, Y. T. Hsieh, N. M. Tsai, P. J. He, W. T. Hsu, Y. C. Yeh, F. H. Chiang, M. S. Wu, C. C. Chang & K. W. Liao, (2009) Characterizing the polymeric status of Helicobacter pylori heat shock protein 60. Biochemical and biophysical research communications 388: 283-289. 263
Lin, Z., D. Madan & H. S. Rye, (2008) GroEL stimulates protein folding through forced unfolding. Nat Struct Mol Biol 15: 303-311. Lindner, R. A., T. M. Treweek & J. A. Carver, (2001) The molecular chaperone alphacrystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin. Biochem J 354: 79-87. Liou, A. K. & K. R. Willison, (1997) Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes. Embo J 16: 4311-4316. Llorca, O., J. Martin-Benito, J. Grantham, M. Ritco-Vonsovici, K. R. Willison, J. L. Carrascosa & J. M. Valpuesta, (2001) The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin. Embo J 20: 4065-4075. Llorca, O., E. A. McCormack, G. Hynes, J. Grantham, J. Cordell, J. L. Carrascosa, K. R. Willison, J. J. Fernandez & J. M. Valpuesta, (1999) Eukaryotic type II chaperonin CCT interacts with actin through specific subunits. Nature 402: 693-696. Lorimer, G. H., (1996) A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo. FASEB J 10: 5-9. Lund, P. A., (2009) Multiple chaperonins in bacteria--why so many? FEMS Microbiol Rev 33: 785-800. Lupas, A. N. & J. Martin, (2002) AAA proteins. Curr Opin Struct Biol 12: 746-753. Maguire, M., A. R. Coates & B. Henderson, (2002) Chaperonin 60 unfolds its secrets of cellular communication. Cell Stress Chaperones 7: 317-329. Maiwald, M., P. W. Lepp & D. A. Relman, (2003) Analysis of conserved non-rRNA genes of Tropheryma whipplei. Syst Appl Microbiol 26: 3-12. 264
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FUNCTIONAL AND STRUCTURAL CHARACTER
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Abstract Proteins are involved in a
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Dedicated to Mum, Dad, and Sharique
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Index of contents Chapter 1: Introd
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2.4.5: Bacteriophage P1 Transductio
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4.1.5: Chimeras DHF & GEI 162 4.2:
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List of illustrations Chapter 1: In
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Fig 4.1: Schematic representation o
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List of tables Chapter 1: Introduct
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SDW STPKs TAE TEMED TBS Sterile dis
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Chapter 1 1.1 Protein Folding The g
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Chapter 1 Fig 1.1: The energy lands
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Chapter 1 To try and escape from th
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Chapter 1 Fig 1.2: Pathways regulat
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Chapter 1 As protein folding in Myc
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Chapter 1 1.4 The molecular chapero
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Chapter 1 1.4.1 Classes of molecula
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Chapter 1 Hsp40 DnaJ CbpA DjlA Ydj1
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Chapter 1 obtained. These revertant
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Chapter 1 1.4.3.1 The ribosome asso
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Chapter 1 (A) (B) Fig 1.7: Structur
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Chapter 1 complete the reaction cyc
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Chapter 1 1.4.3.4 The small Hsps On
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Chapter 1 1.4.3.5 Hsp90 family of c
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Chapter 1 Fig 1.11: Structure of Ht
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Chapter 1 1.4.3.6 Hsp100 family of
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Chapter 1 Fig 1.13: The different r
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Chapter 1 encoded by more than one
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Chapter 1 Fig 1.15: The illustratio
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Chapter 1 (Rommelaere et al., 1993,
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Chapter 1 Fig 1.16: Octameric struc
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Chapter 1 main difference between t
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Chapter 1 1.5.3.3 Prefoldin It has
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Chapter 1 result the substrate prot
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Chapter 1 Fig 1.18: The structures
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Chapter 1 6- If the released peptid
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Chapter 1 1.5.4.3 GroEL substrates
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Chapter 1 Recent work has suggested
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Chapter 1 (A) cpn10 cpn60.1 cpn60.2
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Chapter 1 1998). Cpn60.1 however ha
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Chapter 1 1.6 Aims of the project T
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Chapter 2 Materials and Methods: 2.
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Chapter 2 pET-cpn10- cpn60.1 Deriva
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Chapter 2 2.3 Primers: Below is a l
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Chapter 2 Mut EL.3 Rev groEL 1401-1
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Chapter 2 29R-EL-60.2 groEL 432-412
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Chapter 2 Biofilm base media: 13.6g
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Chapter 2 Preparation of bacterioph
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Chapter 2 then resuspended in 200µ
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Chapter 2 - 10X BSA (depending on t
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Chapter 2 - Colony/culture 1μl - S
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Chapter 2 The PCR cycling parameter
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Chapter 2 tubes were placed on ice
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Chapter 2 2.6 Protein analysis 2.6.
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Chapter 2 2.6.2- Native gel Reagent
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Chapter 2 - Diluted primary antibod
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Chapter 2 supernatant was decanted
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Chapter 2 2.6.6- Analytical ultrace
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Chapter 3 Background As discussed a
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Chapter 3 the -35 region of the trp
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Chapter 3 20 mins 40 mins 60 mins 8
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Chapter 3 (a) 60 mins 90 mins 120 m
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Chapter 3 For this experiment, MGM1
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Chapter 3 When IPTG was not include
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Chapter 3 The results from these co
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Chapter 3 3.2.1 The effect of chang
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Chapter 3 3.2.2 Using pRARE plasmid
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Chapter 3 3.3 Complementation and e
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Chapter 3 of MGM100. The use of Tab
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Chapter 3 3.3.1 Using pET plasmid i
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Chapter 3 1 2 3 4 5 6 7 8 95 kDa 72
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Chapter 3 it only digests the paren
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Chapter 3 72 kDa 1 2 3 4 5 55 kDa 1
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Chapter 3 30°C/26°C 37°C MGM100
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Chapter 3 Fig 3.12: Comparison of t
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Chapter 3 AI90/pACYC-Ptrc-GroESL-Sa
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Chapter 3 1 2 3 4 5 6 7 1000 bp 600
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Chapter 3 10 -1 10 -2 10 -3 10 -4 1
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Chapter 3 this observation. The res
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Chapter 3 expression. However, from
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Chapter 4 Construction and analysis
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Chapter 4 Background In the last ch
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Chapter 4 Experimental design To ma
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Chapter 4 Cpn60.2 7 8 9 Cpn60.1 1 2
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Chapter 4 The full list of all the
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Chapter 4 4.1 Imprecise domain swap
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Chapter 4 4.1.1 Chimera AEC This is
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Chapter 4 (a) Dilutions 10 -1 10 -2
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Chapter 4 of GroEL (fig 4.7). This
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Chapter 4 (a) Dilutions 10 -1 10 -2
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Chapter 4 4.1.5 Chimeras DHF & GEI
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Chapter 4 4.2 Precise domain swaps
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Chapter 4 intermediate domains were
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Chapter 4 1 2 800 kDa 480 kDa 146 k
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Chapter 4 Dilutions 10 -2 10 -3 10
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Chapter 4 is important to note that
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Chapter 4 Summary the complementati
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Chapter 4 The other aspect of this
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Chapter 4 caused due to lack of exp
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Chapter 4 structures were not expec
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Chapter 4 Name Construct Blue -Cpn6
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Chapter 5 Background As discussed i
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Chapter 5 macromolecules at equilib
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Chapter 5 5.1 Purification of JNL 5
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Chapter 5 (a) 1 2 3 4 5 6 7 8 9 10
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Chapter 5 (a) A B C D E (b) 1 2 3 4
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Chapter 5 5.2 AUC analysis of JNL U
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Chapter 5 (a) 1 JNL in Buffer 5 0.9
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Chapter 5 (a) (b) 100 mM P i 75 mM
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Chapter 5 In this experiment GroEL
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Chapter 5 1 2 3 Corrected values Av
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Chapter 5 expected, evidence of lar
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Chapter 5 In summary, based on the
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Chapter 6 In this chapter I will be
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Chapter 6 of Mscpn60.1 can indirect
Page 231 and 232: Chapter 6 can produce products with
Page 233 and 234: Chapter 6 As the group in Pittsburg
Page 235 and 236: Chapter 6 Fig 6.3: Masses of 4 day
Page 237 and 238: Chapter 6 than 7 days, so there is
Page 239 and 240: Chapter 6 are required to facilitat
Page 241 and 242: Chapter 6 Fig 6.4: Sequence alignme
Page 243 and 244: Chapter 6 To ensure that the lack o
Page 245 and 246: Chapter 6 6.2.3 Complementation ana
Page 247 and 248: Chapter 6 Discussion The double rin
Page 249 and 250: Chapter 6 Section 6.3: Testing the
Page 251 and 252: Chapter 6 Experimental design For t
Page 253 and 254: Chapter 6 EcoRV groEL (1.6kb) HindI
Page 255 and 256: Chapter 6 6.3.2 Complementation res
Page 257 and 258: Chapter 6 1 2 3 4 72 kDa 55 kDa Fig
Page 259 and 260: Chapter 6 10 -1 10 -2 10 -3 10 -4 1
Page 261 and 262: Chapter 6 Discussion The results th
Page 263 and 264: Summary The main aim of this study
Page 265 and 266: together, these results strongly su
Page 267 and 268: Basha, E., K. L. Friedrich & E. Vie
Page 269 and 270: Cehovin, A., A. R. Coates, Y. Hu, Y
Page 271 and 272: Diaz-Acosta, A., M. L. Sandoval, L.
Page 273 and 274: Fux, C. A., J. W. Costerton, P. S.
Page 275 and 276: Gupta, P., S. Mishra & T. K. Chaudh
Page 277 and 278: Hoffmann, A., F. Merz, A. Rutkowska
Page 279 and 280: Ito, K., Y. Akiyama, T. Yura & K. S
Page 281: Krzewska, J., G. Konopa & K. Libere
Page 285 and 286: Mogk, A. & B. Bukau, (2004) Molecul
Page 287 and 288: Patzelt, H., G. Kramer, T. Rauch, H
Page 289 and 290: Rommelaere, H., M. Van Troys, Y. Ga
Page 291 and 292: Strickland, E., B. H. Qu, L. Millen
Page 293 and 294: Tyagi, N. K., W. A. Fenton & A. L.
Page 295: Yamamori, T. & T. Yura, (1982) Gene
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