Farnesylation of Pex19p is required for its structural integrity and function in peroxisome biogenesis

Journal of Biological Chemistry

Volumn 284, Issue 31, 2009, Pages 20885-20896

  Rucktäschel, Robert ^a   Thoms, Sven ^a   Sidorovitch, Vadim ^b   Halbach, Andre ^a   Pechlivanis, Markos ^b   Volkmer, Rudolf ^c   Alexandrov, Kirill ^b   Kuhlmann, Jürgen ^b   Rottensteiner, Hanspeter ^b   Erdmann, Ralf ^a  

^a RUHR UNIVERSITY BOCHUM   (Germany)

^b MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

^c CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; ESSENTIAL COMPONENT; FARNESYLATION; FARNESYLTRANSFERASE; GENOMIC MUTATION; IN-VITRO; IN-VIVO; ISOPRENYLATION; LIPID MODIFICATIONS; MATRIX PROTEINS; MEMBRANE ANCHORS; MOLECULAR FUNCTION; PEROXIN; PEROXISOMAL MEMBRANE PROTEIN; PEROXISOME BIOGENESIS; PROTEIN-PROTEIN INTERACTIONS; STEADY-STATE CONCENTRATIONS; SUBSTRATE MEMBRANES; TOPOGENESIS; WILD TYPES;

CYTOLOGY; MACHINERY; PLANTS (BOTANY); PROTEINS;

ENZYME INHIBITION;

FUNGAL PROTEIN; MATRIX PROTEIN; MEMBRANE PROTEIN; PEROXIN 19; PEROXISOMAL MEMBRANE PROTEIN; PROTEIN ANT1P; PROTEIN FARNESYLTRANSFERASE; PROTEIN PEX11; PROTEIN PEX3P; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BIOGENESIS; CONTROLLED STUDY; FARNESYLATION; GENE MUTATION; MOLECULAR RECOGNITION; NONHUMAN; PEROXISOME; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEPLETION; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN PRENYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TARGETING; PROTEIN TRANSPORT; STEADY STATE;

AMINO ACID MOTIFS; CIRCULAR DICHROISM; FARNESYLTRANSTRANSFERASE; MEMBRANE PROTEINS; MUTATION; PEROXISOMES; PRENYLATION; PROTEIN BINDING; PROTEIN SORTING SIGNALS; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 68949092231     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.016584     Document Type: Article

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