Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1992-6-18
pubmed:abstractText
The mitochondrial DNA molecules of two interfertile algal species, Chlamydomonas smithii and C. reinhardtii, are co-linear except for a 1075 bp intron (the alpha-insert) that is present in the cob gene of C. smithii. The alpha-insert, a group I intron (Cs cob.1) containing an open reading frame (ORF) which encodes a basic, hydrophilic protein of 237 amino acids, is unidirectionally transmitted to all diploid progeny during interspecific crosses. In this report, we show that the Cs cob.1-encoded protein is a site-specific endonuclease (I-Csm I) which could mediate the intron transfer via the gene conversion mechanism. The Cs cob.1 ORF was cloned into the vector pMALcr1 and over-expressed as a hybrid protein fused to maltose-binding protein (MBP). This fusion protein exhibited an in vivo endonuclease activity which specifically cleaved the intron homing site within the intronless cob gene.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Algal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Apoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome b Group, http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes b, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Mitochondrial, http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Endonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Maltose-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Catalytic, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0167-4412
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1001-4
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:1316190-Algal Proteins, pubmed-meshheading:1316190-Animals, pubmed-meshheading:1316190-Apoproteins, pubmed-meshheading:1316190-Base Sequence, pubmed-meshheading:1316190-Carrier Proteins, pubmed-meshheading:1316190-Chlamydomonas, pubmed-meshheading:1316190-Cytochrome b Group, pubmed-meshheading:1316190-Cytochromes b, pubmed-meshheading:1316190-DNA, Mitochondrial, pubmed-meshheading:1316190-Endodeoxyribonucleases, pubmed-meshheading:1316190-Endonucleases, pubmed-meshheading:1316190-Gene Conversion, pubmed-meshheading:1316190-Genetic Vectors, pubmed-meshheading:1316190-Introns, pubmed-meshheading:1316190-Maltose-Binding Proteins, pubmed-meshheading:1316190-Molecular Sequence Data, pubmed-meshheading:1316190-Plasmids, pubmed-meshheading:1316190-Polymerase Chain Reaction, pubmed-meshheading:1316190-Protozoan Proteins, pubmed-meshheading:1316190-RNA, Catalytic, pubmed-meshheading:1316190-Recombinant Fusion Proteins
pubmed:year
1992
pubmed:articleTitle
The group I intron of apocytochrome b gene from Chlamydomonas smithii encodes a site-specific endonuclease.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Mississippi State University 39762.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't