Bacteria with increased levels of protein secretion,...

Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives

Reexamination Certificate

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C435S243000, C435S252100, C435S252300, C435S252310, C435S252320, C435S320100, C435S041000, C435S069100, C435S071100, C435S071200, C435S069400, C435S069500, C435S069600, C435S183000, C435S195000, C435S198000, C435S201000, C435S212000, C435S233000, C435S193000, C435S194000, C536S023700

Reexamination Certificate



The invention relates to bacteria that have increased levels of protein secretion due to genetic modification, to nucleotide sequences and gene structures containing at least one gene coding for a SecA protein having increased levels of protein secretion, to a SecA having increased levels of protein secretion, and to a method for producing desired proteins using the inventive bacteria. The invention also relates to nucleic acids coding for a SecA protein having increased levels of protein secretion, containing a SecA gene sequence or allele, a SecA homologue or derivative, or nucleotide sequences hybridising therewith and comprising at least one mutation. Surprisingly, just one mutation in a nucleotide of a SecA gene leads to increased levels of protein secretion or to protein secretion for the first time.

patent: 0 892 064 (1999-01-01), None
patent: 0 892 064 (2000-01-01), None
Baud et al., “Allosteric Communication Between Signal Peptides and the SecA Protein DEAD Motor ATPase Domain,”The Journal of Biological Chemistry, 277(16):13724-13731 (2002).
Freudl et al., “Proteinsekretion bei Gram-positiven Bakterien: Molekulare Grundlagen und biotechnologische Aspekte,” Biospektrum 4(1):29-33 (1998).
Jarosik et al., “Isolation and Analysis of DominantsecA Mutations inEscherichia coli,” Journal of Bacteriology, 173(2):860-868 (1991).
Keilhauer et al., “Isoleucine Synthesis inCorynebacterium glutamicum: Molecular Analysis of theilvB-ilvN-ilvCOperon,”Journal of Bacteriology, 175(17):5595-5603 (1993).
Kisselev, “Polypeptide Release Factors in Prokaryotes and Eukaryotes: Same Function, Different Structure,”Structure, 10: 8-9 (2002).
Klein et al., “Functional Characterization of theStaphylococcus carnosusSecA Protein inEscherichia coliandBacillus subtilissecA Mutant Strains,”FEMS Microbiology Letters, 131:271-277 (1995).
Liebl et al., Transfer ofBrevibacterium divaricatumDSM 20297T, “Brevibacterium flavum” DSM 20411, “Brevibacterium lactofermentum” DSM 20412 and DSM 1412, andCorynebacterium liliumDSM 20137TtoCorynebacterium glutamicumand Their Distinction by rRNA Gene Restriction Patterns,” International Journal of Systematic Bacteriology, 41(2):255-260 (1991).
Matsumoto et al., “Genetic Dissection of SecA: Suppressor Mutations Against thesecY205Translocase defect,”Genes to Cells, 5:991-999 (2000).
Sousa et al., “TheARO4gene ofCandida albicansencodes a tyrosine-sensitive DAHP synthase : evolution, functional conservation and phenotype of Aro3p-, Aro4p-deficient mutants,”Microbiology, 148(Pt5):1291-1303 (2002).
van der Wolk et al., “Identification of the Magnesium-binding Domain of the High-affinity ATP-binding Site of theBacillus subtilisandEscherichia coliSecA Protein,”Journal of Biological Chemistry, 270(32):18975-19892, (1995).
Wishart et al., “A Single Mutation Converts a Novel Phosphotyrosine Binding Domain into a Dual-specificity Phosphatase,”Journal of Biological Chemistry, 270(45):26782-26785, (1995).
Witkowski et al., “Conversion of a β-Ketoacyl Synthase to a Malonyl Decarboxylase by Replacement of the Active-Site Cysteine with Glutamine,”Biochemistry, 38:11643-11650, (1999).


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