Structure-Function Analysis of PrsA Reveals Roles for the Parvulin-like and Flanking N- and C-terminal Domains in Protein Folding and Secretion in Bacillus subtilis

Journal of Biological Chemistry

Volumn 279, Issue 18, 2004, Pages 19302-19314

  Vitikainen, Marika ^a   Lappalainen, Ilkka ^b,c   Seppala, Raili ^a   Antelmann, Haike ^d   Boer, Harry ^e   Taira, Suvi ^b,f   Savilahti, Harri ^d   Hecker, Michael ^d   Vihinen, Mauno ^c,g   Sarvas, Matti ^a   Kontinen, Vesa P ^a  

^a NATIONAL PUBLIC HEALTH INSTITUTE   (Finland)

^b UNIVERSITY OF HELSINKI   (Finland)

^c UNIVERSITY OF TAMPERE   (Finland)

^d UNIVERSITY OF GREIFSWALD   (Germany)

^e VTT TECHNICAL RESEARCH CENTRE OF FINLAND   (Finland)

^f UNIVERSITY OF HELSINKI   (Finland)

^g TAMPERE UNIVERSITY HOSPITAL   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; PROTEINS;

LIPOPROTEINS; PEPTIDE INSERTION;

BIOCHEMISTRY;

AMINO ACID; BACTERIAL PROTEIN; CYCLOPHILIN; MEMBRANE PROTEIN; PARVULIN; PROTEIN; PROTEIN PRSA; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BACILLUS SUBTILIS; BACTERIAL GROWTH; CARBOXY TERMINAL SEQUENCE; CELL WALL; CONTROLLED STUDY; DNA FLANKING REGION; ENZYME ACTIVITY; GENE DELETION; GENE INSERTION; IN VITRO STUDY; IN VIVO STUDY; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECRETION; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; CATALYTIC DOMAIN; LIPOPROTEINS; MEMBRANE PROTEINS; MUTAGENESIS, SITE-DIRECTED; PEPTIDYLPROLYL ISOMERASE; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); INSERTION SEQUENCES; POSIBACTERIA;

EID: 2442446271     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M400861200     Document Type: Article

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