Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1988-1-11
pubmed:abstractText
The specific recognition by mitochondria of the precursor of porin and the insertion into the outer membrane were studied with a radiolabeled water-soluble form of porin derived from the mature protein. High-affinity binding sites had a number of 5-10 pmol/mg mitochondrial protein and a ka of 1-5 X 10(8) M-1. Binding was abolished after trypsin pretreatment of mitochondria indicating that binding sites were of protein-aceous nature. Specifically bound porin could be extracted at alkaline pH but not by high salt and was protected against low concentrations of proteinase K. It could be chased to a highly protease resistant form corresponding to mature porin. High-affinity binding sites could be extracted from mitochondria with detergent and reconstituted in asolectin-ergosterol liposomes. Water-soluble porin competed for the specific binding and import of the precursor of the ADP/ATP carrier, an inner membrane protein. We suggest that (i) binding of precursors to proteinaceous receptors serves as an initial step for recognition, (ii) the receptor for porin may also be involved in the import of precursors of inner membrane proteins, and (iii) interaction with the receptor triggers partial insertion of the precursor into the outer membrane.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-14907713, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-156831, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-215405, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-2878825, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-2884042, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-2989279, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-2998756, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-3015598, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-3034898, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-3036490, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-4066702, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-4093445, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-4435710, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-450112, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-543547, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-6210532, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-6213410, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-6237909, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-6290213, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-6290266, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-6296816, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-6308663, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-6323427, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-6330086, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-6339485, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-7354054, http://linkedlifedata.com/resource/pubmed/commentcorrection/2960520-942051
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2635-42
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
High-affinity binding sites involved in the import of porin into mitochondria.
pubmed:affiliation
Institut für Physiologische Chemie, Universität München, FRG.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't