Linked Life Data

12427759

Source:http://linkedlifedata.com/resource/pubmed/id/12427759

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-1-20
pubmed:abstractText
Dolichol phosphate-mannose (Dol-P-Man) is a mannose donor in various eukaryotic glycosylation processes. So far, two groups of Dol-P-Man synthases have been characterized based on the way they are stabilized in the endoplasmic reticulum membrane. Enzymes belonging to the first group, such as the yeast Dpm1, are typical integral membrane proteins harboring a transmembrane segment (TMS) at their C terminus. In contrast, mammalian Dpm1, enzymes of the second group, lack the typical TMS and require the association with the small hydrophobic proteins Dpm3 to be properly stabilized in the endoplasmic reticulum membrane. In Mycobacterium tuberculosis, the Polyprenol-P-Man synthase MtPpm1 is involved in the biosynthesis of the cell wall-associated glycolipid lipoarabinomannan. MtPpm1 is composed of two domains. The C-terminal catalytic domain is homologous to eukaryotic Dol-P-Man synthases. The N-terminal domain of MtPpm1 contains six TMS that anchor the enzyme in the cytoplasmic membrane. In contrast, in Mycobacterium smegmatis, orthologs of the two domains of MtPpm1 are encoded by two distinct open reading frames, Msppm1 and Msppm2, organized as an operon. No TMS are predicted in MsPpm1, and subcellular fractionation experiments indicate that this enzyme is cytosolic when produced in Escherichia coli. Computer-assisted topology predictions and alkaline phosphatase insertions showed that MsPpm2 is an integral membrane protein. Using a recently developed bacterial two-hybrid system, it was found that MsPpm2 interacts with MsPpm1 to stabilize the synthase MsPpm1 in the bacterial membrane. This interaction is reminiscent of that of mammalian Dpm1 with Dpm3 and mimics the structure of MtPpm1 as demonstrated by the capacity of the two domains of MtPpm1 to spontaneously interact when co-expressed in E. coli.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2242-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12427759-Alkaline Phosphatase, pubmed-meshheading:12427759-Amino Acid Sequence, pubmed-meshheading:12427759-Bacterial Proteins, pubmed-meshheading:12427759-Cell Membrane, pubmed-meshheading:12427759-Cyclin-Dependent Kinases, pubmed-meshheading:12427759-Databases as Topic, pubmed-meshheading:12427759-Dolichol Monophosphate Mannose, pubmed-meshheading:12427759-Escherichia coli, pubmed-meshheading:12427759-Escherichia coli Proteins, pubmed-meshheading:12427759-Mannosyltransferases, pubmed-meshheading:12427759-Models, Biological, pubmed-meshheading:12427759-Models, Genetic, pubmed-meshheading:12427759-Molecular Sequence Data, pubmed-meshheading:12427759-Mycobacterium smegmatis, pubmed-meshheading:12427759-Plasmids, pubmed-meshheading:12427759-Polyisoprenyl Phosphate Monosaccharides, pubmed-meshheading:12427759-Protein Structure, Tertiary, pubmed-meshheading:12427759-Two-Hybrid System Techniques
pubmed:year
2003
pubmed:articleTitle
In vivo interaction between the polyprenol phosphate mannose synthase Ppm1 and the integral membrane protein Ppm2 from Mycobacterium smegmatis revealed by a bacterial two-hybrid system.
pubmed:affiliation
INSERM U447, Institut Pasteur de Lille - Institut de Biologie de Lille, France. alain.baulard@pasteur-lille.fr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't