WO2003058197A3 - Detection of molecular interactions by beta-lactamase reporter fragment complementation - Google Patents

Detection of molecular interactions by beta-lactamase reporter fragment complementation Download PDF

Info

Publication number
WO2003058197A3
WO2003058197A3 PCT/US2002/041587 US0241587W WO03058197A3 WO 2003058197 A3 WO2003058197 A3 WO 2003058197A3 US 0241587 W US0241587 W US 0241587W WO 03058197 A3 WO03058197 A3 WO 03058197A3
Authority
WO
WIPO (PCT)
Prior art keywords
interactions
protein
detection
lactamase
molecular interactions
Prior art date
Application number
PCT/US2002/041587
Other languages
French (fr)
Other versions
WO2003058197A2 (en
Inventor
Helen M Blau
Robert F Balint
Thomas S Wehrman
Jeng-Horng Her
Original Assignee
Univ Leland Stanford Junior
Helen M Blau
Robert F Balint
Thomas S Wehrman
Jeng-Horng Her
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Univ Leland Stanford Junior, Helen M Blau, Robert F Balint, Thomas S Wehrman, Jeng-Horng Her filed Critical Univ Leland Stanford Junior
Priority to AU2002364250A priority Critical patent/AU2002364250A1/en
Publication of WO2003058197A2 publication Critical patent/WO2003058197A2/en
Publication of WO2003058197A3 publication Critical patent/WO2003058197A3/en

Links

Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/536—Immunoassay; Biospecific binding assay; Materials therefor with immune complex formed in liquid phase
    • G01N33/542—Immunoassay; Biospecific binding assay; Materials therefor with immune complex formed in liquid phase with steric inhibition or signal modification, e.g. fluorescent quenching
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/90—Enzymes; Proenzymes
    • G01N2333/914—Hydrolases (3)
    • G01N2333/978—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
    • G01N2333/986—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5) acting on amide bonds in cyclic amides (3.5.2), e.g. beta-lactamase (penicillinase, 3.5.2.6), creatinine amidohydrolase (creatininase, EC 3.5.2.10), N-methylhydantoinase (3.5.2.6)

Landscapes

  • Health & Medical Sciences (AREA)
  • Immunology (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Molecular Biology (AREA)
  • Biomedical Technology (AREA)
  • Chemical & Material Sciences (AREA)
  • Hematology (AREA)
  • Urology & Nephrology (AREA)
  • Biotechnology (AREA)
  • Microbiology (AREA)
  • Cell Biology (AREA)
  • Food Science & Technology (AREA)
  • Medicinal Chemistry (AREA)
  • Physics & Mathematics (AREA)
  • Analytical Chemistry (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • General Physics & Mathematics (AREA)
  • Pathology (AREA)
  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)

Abstract

Methods and compositions for detecting molecular interactions, particularly, protein-protein interactions, using at least two inactive, weakly-complementing ß-lactamase fragments are provided. The invention allows detection of such interactions in eukaryotic and mammalian cells, in situ or in vitro. Detection of molecular interactions in mammalian cells is not limited to the nuclear compartment, but can be accomplished in the cytoplasm, cell surface, organelles, or between these entities. Methods provided utilize novel compositions comprising fusion proteins between molecules of interest and inactive, weakly-complementing-ßlactamase fragments. Association of the molecules of interest brings the corresponding complementary ß-lactamase fragments into close enough proximity for complementation to occur and ß-lactamase activity to be observed. The invention is useful in the study of protein-protein interactions, functional genomics, agonist and antagonist screening and drug discovery.
PCT/US2002/041587 2001-12-26 2002-12-26 Detection of molecular interactions by beta-lactamase reporter fragment complementation WO2003058197A2 (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
AU2002364250A AU2002364250A1 (en) 2001-12-26 2002-12-26 Detection of molecular interactions by beta-lactamase reporter fragment complementation

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US34475701P 2001-12-26 2001-12-26
US60/344,757 2001-12-26

Publications (2)

Publication Number Publication Date
WO2003058197A2 WO2003058197A2 (en) 2003-07-17
WO2003058197A3 true WO2003058197A3 (en) 2004-01-22

Family

ID=23351896

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/US2002/041587 WO2003058197A2 (en) 2001-12-26 2002-12-26 Detection of molecular interactions by beta-lactamase reporter fragment complementation

Country Status (2)

Country Link
AU (1) AU2002364250A1 (en)
WO (1) WO2003058197A2 (en)

Families Citing this family (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8148110B2 (en) 1999-03-15 2012-04-03 The Board Of Trustees Of The Leland Stanford Junior University Detection of molecular interactions by β-lactamase reporter fragment complementation
US8586294B2 (en) * 2004-05-18 2013-11-19 The Board Of Trustees Of The Leland Stanford Junior University Detection of protein translocation by beta-galactosidase reporter fragment complementation
EP1847604A1 (en) * 2006-04-19 2007-10-24 Millegen Intracellular method for selecting a peptide or polypeptide which binds to a bait peptide or polypeptide
US8426138B2 (en) 2006-12-26 2013-04-23 The Board Of Trustees Of The Leland Stanford Junior University Detection of sub-cellular compartment localization of a molecule using a reduced affinity enzyme complementation reporter system
US8101373B2 (en) 2007-10-12 2012-01-24 Discoverx Corporation β-galactosidase donor fragments

Non-Patent Citations (4)

* Cited by examiner, † Cited by third party
Title
CHERVAUX C. ET AL.: "Secretion of active beta-lactamase to the medium mediated by the escherichia coli haemolysin transport pathway", MOL. GEN. GENET., vol. 249, 1995, pages 237 - 245, XP002963973 *
JAMSA E. ET AL.: "In vivo reactivation of heat-denatured protein in the endoplasmic reticulum of yeast", THE EMBO J., vol. 14, no. 23, 1995, pages 6028 - 6033, XP002963974 *
SIMONEN M. ET AL.: "The role of the carrier protein and disulfide formation in the folding of beta-lactamase fusion proteins in the endoplasmic reticulum of yeast", J. BIOL. CHEM., vol. 269, no. 19, 13 May 1994 (1994-05-13), pages 13887 - 13892, XP002963975 *
WARD V.K. ET AL.: "Generation of an expression library in the baculovirus expression vector system", J. VIROLOGICAL METHODS, vol. 53, 1995, pages 263 - 272, XP002210406 *

Also Published As

Publication number Publication date
AU2002364250A8 (en) 2003-07-24
AU2002364250A1 (en) 2003-07-24
WO2003058197A2 (en) 2003-07-17

Similar Documents

Publication Publication Date Title
Ossareh‐Nazari et al. Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required for ribophagy
Dix et al. Global mapping of the topography and magnitude of proteolytic events in apoptosis
Nathan et al. Why do cellular proteins linked to K63‐polyubiquitin chains not associate with proteasomes?
Schmidt et al. Endosome and Golgi‐associated degradation (EGAD) of membrane proteins regulates sphingolipid metabolism
Tsuchiya et al. Ub-ProT reveals global length and composition of protein ubiquitylation in cells
Ma et al. Livin promotes Smac/DIABLO degradation by ubiquitin–proteasome pathway
Verma et al. Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26 S proteasome
Moresco et al. Identifying components of protein complexes in C. elegans using co-immunoprecipitation and mass spectrometry
Back et al. Site-specific K63 ubiquitinomics provides insights into translation regulation under stress
Chan et al. Ubiquitination of p53 at multiple sites in the DNA-binding domain
Williamson et al. The Colossus of ubiquitylation: decrypting a cellular code
Oshikawa et al. Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin
WO2003048300A3 (en) Methods of identifying cellular target molecules
Neal et al. A Cdc48 “retrochaperone” function is required for the solubility of retrotranslocated, integral membrane endoplasmic reticulum-associated degradation (ERAD-M) substrates
Jung et al. Modulating cellular balance of Rps3 mono-ubiquitination by both Hel2 E3 ligase and Ubp3 deubiquitinase regulates protein quality control
Li et al. Proteasomes: isolation and activity assays
Maurer et al. Combining filter-aided sample preparation and pseudoshotgun technology to profile the proteome of a low number of early passage human melanoma cells
O’Connor et al. Enzyme–substrate relationships in the ubiquitin system: approaches for identifying substrates of ubiquitin ligases
WO2006107813A3 (en) Site specific incorporation of phosphoserine into polypeptides using phosphoseryl-trna synthetase
Yang et al. The chaperone Tsr2 regulates Rps26 release and reincorporation from mature ribosomes to enable a reversible, ribosome-mediated response to stress
WO2004024750A3 (en) Cd44-binding ligands
WO2005113838A3 (en) Detection of protein translocation by beta-galactosidase reporter fragment complementation
Brands et al. Ctf7p/Eco1p exhibits acetyltransferase activity–but does it matter?
WO2003058197A3 (en) Detection of molecular interactions by beta-lactamase reporter fragment complementation
WO2007050584A3 (en) Detection of intracellular enzyme complex

Legal Events

Date Code Title Description
AK Designated states

Kind code of ref document: A2

Designated state(s): AE AG AL AM AT AU AZ BA BB BG BR BY BZ CA CH CN CO CR CU CZ DE DK DM DZ EC EE ES FI GB GD GE GH GM HR HU ID IL IN IS JP KE KG KP KR KZ LC LK LR LS LT LU LV MA MD MG MK MN MW MX MZ NO NZ OM PH PL PT RO RU SC SD SE SG SK SL TJ TM TN TR TT TZ UA UG US UZ VC VN YU ZA ZM ZW

AL Designated countries for regional patents

Kind code of ref document: A2

Designated state(s): GH GM KE LS MW MZ SD SL SZ TZ UG ZM ZW AM AZ BY KG KZ MD RU TJ TM AT BE BG CH CY CZ DE DK EE ES FI FR GB GR IE IT LU MC NL PT SE SI SK TR BF BJ CF CG CI CM GA GN GQ GW ML MR NE SN TD TG

121 Ep: the epo has been informed by wipo that ep was designated in this application
DFPE Request for preliminary examination filed prior to expiration of 19th month from priority date (pct application filed before 20040101)
122 Ep: pct application non-entry in european phase
NENP Non-entry into the national phase

Ref country code: JP

WWW Wipo information: withdrawn in national office

Country of ref document: JP