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rdf:type |
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lifeskim:mentions |
umls-concept:C0040715,
umls-concept:C0162326,
umls-concept:C0542341,
umls-concept:C0599718,
umls-concept:C0599813,
umls-concept:C0599893,
umls-concept:C1514562,
umls-concept:C1522702,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2825490
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pubmed:issue |
2
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pubmed:dateCreated |
2006-1-12
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pubmed:abstractText |
In topogenesis of membrane proteins on the endoplasmic reticulum, the orientation of the hydrophobic transmembrane (TM) segment is influenced by the charge of the flanking amino acid residues. We assessed the function of the positive charges downstream of the hydrophobic segment using synaptotagmin II. The positive charges were systematically replaced with non-charged residues. Although the original TM segment translocated the N terminus, the topology was inverted, depending on the mutations. Orientation was affected in mutants in which 6 Lys were shifted downstream, even when the 6 Lys were 25 residues from the hydrophobic segment. The Lys was functionally replaced by Arg, but not by Asp or Glu. The timing of action during polypeptide elongation indicated that the Lys functions at the ribosome exit sites. We suggest that the commitment of the TM segment to a particular orientation is influenced by far downstream parts of the polypeptide chain and that the positive charges are decoded after exiting the ribosome.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Cycloheximide,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Synthesis Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmin II
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1152-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16291756-Amino Acid Sequence,
pubmed-meshheading:16291756-Animals,
pubmed-meshheading:16291756-Arginine,
pubmed-meshheading:16291756-Aspartic Acid,
pubmed-meshheading:16291756-COS Cells,
pubmed-meshheading:16291756-Cercopithecus aethiops,
pubmed-meshheading:16291756-Cluster Analysis,
pubmed-meshheading:16291756-Cycloheximide,
pubmed-meshheading:16291756-DNA, Complementary,
pubmed-meshheading:16291756-Dogs,
pubmed-meshheading:16291756-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:16291756-Endoplasmic Reticulum,
pubmed-meshheading:16291756-Gene Deletion,
pubmed-meshheading:16291756-Glutamic Acid,
pubmed-meshheading:16291756-Glycosylation,
pubmed-meshheading:16291756-Lysine,
pubmed-meshheading:16291756-Mice,
pubmed-meshheading:16291756-Microsomes,
pubmed-meshheading:16291756-Models, Biological,
pubmed-meshheading:16291756-Molecular Sequence Data,
pubmed-meshheading:16291756-Mutation,
pubmed-meshheading:16291756-Peptides,
pubmed-meshheading:16291756-Plasmids,
pubmed-meshheading:16291756-Protein Conformation,
pubmed-meshheading:16291756-Protein Structure, Tertiary,
pubmed-meshheading:16291756-Protein Synthesis Inhibitors,
pubmed-meshheading:16291756-Protein Transport,
pubmed-meshheading:16291756-RNA, Messenger,
pubmed-meshheading:16291756-Rabbits,
pubmed-meshheading:16291756-Ribosomes,
pubmed-meshheading:16291756-Sequence Homology, Amino Acid,
pubmed-meshheading:16291756-Synaptotagmin II,
pubmed-meshheading:16291756-Transcription, Genetic
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pubmed:year |
2006
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pubmed:articleTitle |
Function of positive charges following signal-anchor sequences during translocation of the N-terminal domain.
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pubmed:affiliation |
Core Research for Evolutional Science and Technology (CREST) of the Japan Science and Technology Agency, Hyogo.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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