Matches in SemOpenAlex for { <https://semopenalex.org/work/W3009904504> ?p ?o ?g. }
Showing items 1 to 61 of
61
with 100 items per page.
- W3009904504 abstract "Although chaperonin-assisted protein folding has been studied in vitro by a number of investigators, the features of an unfolded or partially folded polypeptide that are recognized and bound by chaperonins are not known. I addressed this question using the precursor of the small subunit (pS) of ribulose-1,5-bisphosphate carboxylase as a model substrate for GroEL, the bacterial chaperonin. The precursor protein was expressed in E. coli as a C-terminal fusion to protein A. Protein A-pS (and any associated cellular proteins) was isolated by affinity chromatography. GroEL could be eluted from the fusion protein by ATP and either GroES or casein, consistent with results of in vitro folding assays. Using deletions from the C-terminus of pS I defined the smallest truncation of pS, PAxpS90T, that binds GroEL with high avidity. A series of site-specific mutations targeting the C-terminal 15-20 amino acids of PAxpS90T was constructed and analyzed for the ability to bind GroEL. Two of these mutations bound significantly less GroEL than PAxpS90T, suggesting that this region is required for avid GroEL binding. I demonstrated a physical interaction between GroEL and this region of pS with a novel assay that utilizes the protection of tyrosine residues from iodination upon formation of specific protein-protein complexes. Finally, I further showed that at least half of the transit sequence of pS is also required for avid binding to GroEL. The association constants for the interaction of GroEL with PAxpS, PAxpS90T, or its mutated derivatives, were determined and fell within the range $3.7times10sp7$ to $2.7times 10sp6$ M$sp{-1}$. Analysis of the affinity constants for PAxpS90T mutants allowed us to define a possible recognition motif for GroEL's interaction with pS. This motif includes the recognition of both hydrophobic and positively charged amino acids. The motif need not be helical, but structural rigidity may be a requirement for recognition (and binding) by GroEL." @default.
- W3009904504 created "2020-03-13" @default.
- W3009904504 creator A5038627142 @default.
- W3009904504 date "2022-06-14" @default.
- W3009904504 modified "2023-10-07" @default.
- W3009904504 title "Specificity of Chaperonin GroEL Binding to the Precursor of the Small Subunit of Ribulose-1,5-Bisphosphate Carboxylase." @default.
- W3009904504 doi "https://doi.org/10.31390/gradschool_disstheses.5494" @default.
- W3009904504 hasPublicationYear "2022" @default.
- W3009904504 type Work @default.
- W3009904504 sameAs 3009904504 @default.
- W3009904504 citedByCount "0" @default.
- W3009904504 crossrefType "dissertation" @default.
- W3009904504 hasAuthorship W3009904504A5038627142 @default.
- W3009904504 hasBestOaLocation W30099045041 @default.
- W3009904504 hasConcept C104292427 @default.
- W3009904504 hasConcept C104317684 @default.
- W3009904504 hasConcept C123894998 @default.
- W3009904504 hasConcept C153911025 @default.
- W3009904504 hasConcept C181199279 @default.
- W3009904504 hasConcept C185592680 @default.
- W3009904504 hasConcept C204328495 @default.
- W3009904504 hasConcept C40767141 @default.
- W3009904504 hasConcept C46522908 @default.
- W3009904504 hasConcept C50212798 @default.
- W3009904504 hasConcept C547475151 @default.
- W3009904504 hasConcept C55493867 @default.
- W3009904504 hasConcept C85755625 @default.
- W3009904504 hasConcept C86803240 @default.
- W3009904504 hasConcept C87190427 @default.
- W3009904504 hasConceptScore W3009904504C104292427 @default.
- W3009904504 hasConceptScore W3009904504C104317684 @default.
- W3009904504 hasConceptScore W3009904504C123894998 @default.
- W3009904504 hasConceptScore W3009904504C153911025 @default.
- W3009904504 hasConceptScore W3009904504C181199279 @default.
- W3009904504 hasConceptScore W3009904504C185592680 @default.
- W3009904504 hasConceptScore W3009904504C204328495 @default.
- W3009904504 hasConceptScore W3009904504C40767141 @default.
- W3009904504 hasConceptScore W3009904504C46522908 @default.
- W3009904504 hasConceptScore W3009904504C50212798 @default.
- W3009904504 hasConceptScore W3009904504C547475151 @default.
- W3009904504 hasConceptScore W3009904504C55493867 @default.
- W3009904504 hasConceptScore W3009904504C85755625 @default.
- W3009904504 hasConceptScore W3009904504C86803240 @default.
- W3009904504 hasConceptScore W3009904504C87190427 @default.
- W3009904504 hasLocation W30099045041 @default.
- W3009904504 hasOpenAccess W3009904504 @default.
- W3009904504 hasPrimaryLocation W30099045041 @default.
- W3009904504 hasRelatedWork W1970978994 @default.
- W3009904504 hasRelatedWork W1995792761 @default.
- W3009904504 hasRelatedWork W2016135054 @default.
- W3009904504 hasRelatedWork W2016698833 @default.
- W3009904504 hasRelatedWork W2032157978 @default.
- W3009904504 hasRelatedWork W2035292024 @default.
- W3009904504 hasRelatedWork W2063513185 @default.
- W3009904504 hasRelatedWork W2113034025 @default.
- W3009904504 hasRelatedWork W2147289825 @default.
- W3009904504 hasRelatedWork W94733720 @default.
- W3009904504 isParatext "false" @default.
- W3009904504 isRetracted "false" @default.
- W3009904504 magId "3009904504" @default.
- W3009904504 workType "dissertation" @default.