Overexpression of L-Isoaspartate O-Methyltransferase in Escherichia coli Increases Heat Shock Survival by a Mechanism Independent of Methyltransferase Activity

Journal of Biological Chemistry

Volumn 278, Issue 51, 2003, Pages 50880-50886

  Kindrachukt, Jason ^a,b   Parent, Jennifer ^a   Davies, Gerald F ^a   Dinsmore, Michael ^a   Attah Poku, Samuel ^b   Napper, Scott ^a,b  

^a UNIVERSITY OF SASKATCHEWAN   (Canada)

^b UNIVERSITY OF SASKATCHEWAN   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL MODIFICATION; ENZYMES; GENETIC ENGINEERING; PHYSIOLOGY; REACTION KINETICS; THERMAL STRESS;

HEAT TOLERANCE; HOMOLOGY;

ESCHERICHIA COLI;

ISOASPARTATE O METHYLTRANSFERASE; ISOASPARTIC ACID; METHYLTRANSFERASE; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CATALYSIS; CELL SURVIVAL; COVALENT BOND; CYCLIZATION; DEAMINATION; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE MUTATION; GENE OVEREXPRESSION; GENETIC CONSERVATION; ISOMERISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; HEAT-SHOCK RESPONSE; HSP70 HEAT-SHOCK PROTEINS; KINETICS; MUTATION; PROTEIN BINDING; PROTEIN D-ASPARTATE-L-ISOASPARTATE METHYLTRANSFERASE; SEQUENCE ALIGNMENT; TRANSDUCTION, GENETIC;

ANIMALIA; BACTERIA (MICROORGANISMS); DROSOPHILA MELANOGASTER; ESCHERICHIA COLI; MELANOGASTER;

EID: 0347065369     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M308423200     Document Type: Article

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