Nucleotide sequences coding for the cls gene

Details Nucleotide sequences coding for the cls gene Nucleotide sequences coding for the cls gene

2001-05-04

2003-05-13

Achutamurthy, Ponnathapu (Department: 1652)

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

C536S023200, C536S024300, C536S024320, C435S252320, C435S320100

Reexamination Certificate

active

06562607

ABSTRACT:

The invention provides genetically modified coryneform bacteria, nucleotide sequences coding for cardiolipin synthase and a process for the fermentative production of amino acids, in particular L-glutamate, using coryneform bacteria, in which the cls gene, which codes for cardiolipin synthase, is amplified. All references cited herein are expressly incorporated by reference. Incorporation by reference is also designated by the term “I.B.R.” following any citation.
PRIOR ART
Amino acids, in particular L-glutamate, are used in human medicine, in animal nutrition and in the pharmaceuticals industry, but in particular in the foodstuffs industry.
It is known that amino acids are produced by fermentation of strains of coryneform bacteria, in particular
Corynebacterium glutamicum.
Due to their great significance, efforts are constantly being made to improve the production process. Improvements to the process may relate to measures concerning fermentation technology, for example stirring and oxygen supply, or to the composition of the nutrient media, such as for example sugar concentration during fermentation, or to working up to yield the product by, for example, ion exchange chromatography, or to the intrinsic performance characteristics of the microorganism itself.
The performance characteristics of these microorganisms are improved using methods of mutagenesis, selection and mutant selection.
For some years, methods of recombinant DNA technology have moreover been used to improve strains of Corynebacterium which produce amino acids by amplifying individual amino acid biosynthesis genes and investigating the effect on amino acid production. Review articles on this subject may be found inter alia in Kinoshita (“Glutamic Acid Bacteria”, in: Biology of Industrial Microorganisms, Demain and Solomon (Eds.) I.B.R., Benjamin Cummings, London, UK, 1985, 115-142) I.B.R., Hilliger (BioTec 2, 40-44 (1991)) I.B.R., Eggeling (Amino Acids 6:261-272 (1994)) I.B.R., Jetten and Sinskey (Critical Reviews in Biotechnology 15, 73-103 (1995)) I.B.R. and Sahm et al. (Annuals of the New York Academy of Science 782, 25-39 (1996)) I.B.R.
OBJECT OF THE INVENTION
The object of the present invention was to provide novel auxiliaries for the improved fermentative production of amino acids, in particular L-glutamate.
Amino acids, in particular L-glutamate, are used in human medicine, in animal nutrition, in the pharmaceuticals industry, and in particular in the foodstuffs industry. There is accordingly general interest in providing novel improved processes for the production of amino acids, in particular L-glutamate.
Any subsequent mention of L-glutamate or glutamate should be taken to mean not only the base, but also the salts thereof.
SUMMARY OF THE INVENTION
The new DNA sequence of
C. glutamicum
which codes for the cls gene and which as a constituent of the present invention is SEQ ID NO 1 and related sequences. The amino acid sequence of the corresponding gene product of the cls gene has furthermore been derived from the present DNA sequence. The resulting amino acid sequence of the cls gene product is SEQ ID NO 2 and related sequences.


REFERENCES:
patent: 0 771 879 (1997-05-01), None
patent: 1 108 790 (2001-06-01), None
patent: WO 01/00805 (2001-01-01), None
Ohta A. et al. Molecular cloning of the csl gene responsible for cardiolipin synthesis inE. coliand phenotipic consequences of its amplification, J. Bacteriol. (1985), 163, 506-514.*
Nishijima S. et al. Disruption ofEscherichia colicls gene responsible for cardiolipin synthesis, J. Bacteriol. (1988), 170, 774-780.*
Hiraoka S. et al. Amplification and substantial purification of cardiolipin synthase ofE. coli.J. Biochem. (1991), 110, 443-449.*
Ragolia L. et al. The effects of phosphoglycerides onEscherichia colicardiolipin synthase, Biochim. Biophys Acta, (1994), 1214, 323-332.*
Tropp B. E. Cardiolipin synthase fromEscherichia coli, Biochim. Biophys. Acta (1997), 1348, 192-200.*
L. Eggeling, et al., “L-Glutamate and L-lysine: Traditional Products with Impetuous Developments,” Applied Microbiology and Biotechnology, Aug. 8, 1999, vol. 52, pp. 146-153.
International Search Report for counterpart application No. PCT/EP''''''''''''''''''''''''''''''01/04705, dated Nov. 22, 2001.

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