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    Protein Production for

    Structural InvestigationsBased on a Wheat Germ

    Cell-Free Expression System

    John L. Markley

    [email protected]

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    Where cell-free fits in the big picture of CESG

    Please see the CESG posters

    1. Pipeline overview

    2. Constructs, E. colistrains and media (Terrific Broth

    & chemically-defined), and expression screening

    3. Large-scale E. colicell growth and protein

    purification

    4. Efficient labeling (Se-Met,

    15

    N, &

    13

    C;

    15

    N) of proteinsproduced from E. coli

    5. High-throughput crystallomics

    6. Cell-free protein production: expression screening &

    production of labeled proteins

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    Target selection

    E. colicells

    Screening: expression & solubility

    Cell-free

    Screening: expression & solubility

    13C,15N-

    label

    Small

    proteins:15N label

    Large

    proteins:

    Se-Met

    Large-scale growth & purification

    Small

    proteins:15N label

    Large

    proteins:

    Large-scale growth & purification

    13C,15N-

    labelSe-Met-

    label

    NMRX-ray

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    Target

    Cloning Production & analysis of15N-protein

    PCR from cDNA DNA plasmid preps

    Ligation cloning TranscriptionDNA plasmid preps Translation on [15N]-amino acids

    (4 ml reaction)

    Small scale (50 Ql reaction) Isolation, purification (tag removal)

    Transcription HSQC NMR analysis

    Translation Solubility, stability, & MS analysis

    Analysis Production of [13C,15N]-protein

    Expression level As above but with double-labeling

    Solubility (4 12 ml reaction)

    (Tag cleavage)

    Structure determination

    Work-flow diagram: wheat germ cell-free approach for NMR

    Screening Production for structural analysis

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    Solubility of (His)6-fusions

    High ( >50 %) 75 65 %

    Low (< 50 %) 41 35 %

    Total 116 100 %

    Small scale (50 Ql) results:

    Arabidopsis ORFs with N-terminal (His)6 tags

    Overall success rate for producing highly soluble protein with

    N-terminal (His)6tag: 50%

    Expression

    Yes 116 77 %

    No 35 23 %

    Total 151 100 %

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    80 (both)

    52 (both)

    Expressed: 89 total

    Soluble: 63 total

    3 6

    7 4

    GST-fusion

    GST-fusion

    after cleavage

    (His)6-fusion

    (His)6-fusion

    Screening results:

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    Large scale cell-free production for structural studiesN-(His)6 tag N-GST tag

    Number of proteins ([15N]-, 4 ml rxn): 49 3

    Low yield (no HSQC) 26 (54 %) 0 (0 %)

    Higher yield (HSQC possible) 23 (46 %) 3 (100 %)Average yield: 0.6 mg/ml 0.75 mg/ml

    (following

    cleavage)

    1N-15N HSQC results:

    + (folded, non-aggregating) 14 (61 %) 1 (33 %)

    - (unsuitable for NMR structure) 9 (39 %) 2 (67 %)

    Number of proteins ([13C,15N]-, 4-12 ml rxn): 5 1

    Structures solved 2 -

    Structures in progress 3 1

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    Robotics: CFS GeneDecoder 1000: delivered January 2004

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    Two modes of operation for the GeneDecoder 1000

    Screening

    Uses 4 x 96-well plates

    Overnight run Produces 2-10 Qg protein / well

    Consumes 2.5 5 mL of wheat germ extract / plate

    Small-scale protein production

    Uses 2 x 96-well plates

    Overnight run

    Produces 10-50 Qg protein / well

    Consumes 5 10 mL of wheat germ extract / plate

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    Preliminary results from the Comparison Workgroup of96 Arabidopsis targets: (1) small-scale expression trials

    E. colicells

    Total tested 95All MBP-fusions

    Expression 39

    Expression + 56

    (59 %)

    Insoluble 1

    Soluble 55

    (58 %)

    Wheat germ cell-free

    Total tested 93 90Fusion: (His)6 GST

    Expression 11 11

    Expression + 82 79

    (88 %) (88 %)

    Insoluble 30 35

    Cleavage - 1

    Cleavage + - 43

    Soluble 52 44

    (56 %) (48 %)

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    SummaryAdvantages

    Cell-free method supports rapid and efficient screening

    (supported by robotics)

    Cell-free method requires smaller volumes (avoids lengthy

    concentration steps in protein purification)

    Labeled proteins can be prepared rapidly (in 1-2 days) to meetneeds of structural biologists

    Supports labeling strategies that are not practical for proteins

    produced from bacterial cells (no label scrambling)

    Supports the production of eukaryotic N-terminal (His)6 proteins

    (previous experience showed that these were not produced

    successfully from E. colicells)

    Disadvantages

    Reagent intensive

    Currently not compatible with Gateway cloning technology used

    in other parts of the project

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    32 kD CESG target: protein madein Tokyo by E. colicell-free; NMRstructure solved in Tokyo

    Future cell-free plansRobotics

    Automate the protein production (12 4-6 ml reactions / week)

    Large-scale robot to be delivered by May 2004

    Se-Met samples for X-ray crystallography

    Successful for 3 proteins on a 50 Ql scale

    Stereo array isotope labeling (SAIL) from wheat germ cell-free

    Collaboration with M. Kainosho (Tokyo Metro. Univ.)

    Complete the Comparison Workgroup96 targets produced from E. colicells and wheat germ cell free

    E. colicells part complete (through 1H-15N HSQC of MBP-cleaved)

    Cell-free screening nearly complete (His6- and GST-cleaved)

    Cell-free 1H-15N HSQC in progress (His6- and GST-cleaved)

    Targets from other eukaryotic genomes

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    UW-Madison: Dave Aceti, Rick Amasino, Raj Arangarasan, Arash Bahrami, Craig

    Bingman, Paul Blommel, Blake Buchan, Heather Burch, John Cao, Claudia

    Cornilescu, Gabriel Cornilescu, Jurgen Doreleijers, Dave Dyer, Hamid Eghbalnia,

    Brian Fox, Ronnie Fredrick, Holalkere Geetha, Premkum Gopalakrishnan, ByungWoo Han, Adrian Hegeman, Dave Hruby, Won Bae Jeon, Ken Johnson, Todd Kimball,

    Kelly Kjer, John Kunert, Min S. Lee, Peter Lee, Jing Li, Scott Leisman, Miron Livny,

    Andrew Markley, Zach Miller, Ramya Narayama, Craig Newman, George Phillips,

    John Primm, Bryan Ramirez, Nitin Ravoof, Ivan Rayment, Megan Riters, Michael

    Runnels, Kory Seder, Mark Shahan, Jeff Shaw, Shanteri Singh, David Smith, Jikui

    Song, Hassan Sreenath, Mike Sussman, Sandy Thao, Ejan Tyler, Robert Tyer, Eldon

    Ulrich, Dmitriy Vinarov, Frank Vojtik, Liya Wang, R. Kent Wenger, Gary Wesensberg,

    Milo Westler, Russell Wrobel, Jianhua Zhang, Qin Zhao, Zsolt Zolnai

    Medical College of Wisconsin: Betsy Lytle, Brian Volkman, Francis Peterson

    Molecular Kinetics: Keith Dunker, Chris Oldfield

    Hebrew University (Jerusalem): Michal Linial, Elon Portugaly, Ilone Kifer

    German National Center for Health & Environment (Munich): Dmitrij Frishman

    Tokyo Metropolitan University: Masatsune Kainosho, Yuko Katagiri, Nozomi

    Sugimori, Akira M. Ono, Tsutomu Terauchi, Takuya Torizawa

    Ehime University:Yaeta Endo, Tatsuya Sawasaki

    CellFreeSciences, Inc. (Yokohama): Ryo Morishita, Mihoro Saeki,

    Motoo Watanabe

    CESG team members and collaborators

    P50 GM 64598

    Support