Synthesis and Intracellular Transport of Aminoglycerophospholipids in Permeabilized Cells of the Yeast, Saccharomyces cerevisiae(∗)

The sequence of biosynthetic steps from phosphatidylserine to phosphatidylethanolamine (via decarboxylation) and then phosphatidylcholine (via methylation) is linked to the intracellular transport of these aminoglycerophospholipids. Using a [3H]serine precursor and permeabilized yeast cells, it is p...

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Veröffentlicht in:The Journal of biological chemistry 1995-12, Vol.270 (50), p.29836-29842
Hauptverfasser: Achleitner, Georg, Zweytick, Dagmar, Trotter, Pamela J., Voelker, Dennis R., Daum, Günther
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container_end_page 29842
container_issue 50
container_start_page 29836
container_title The Journal of biological chemistry
container_volume 270
creator Achleitner, Georg
Zweytick, Dagmar
Trotter, Pamela J.
Voelker, Dennis R.
Daum, Günther
description The sequence of biosynthetic steps from phosphatidylserine to phosphatidylethanolamine (via decarboxylation) and then phosphatidylcholine (via methylation) is linked to the intracellular transport of these aminoglycerophospholipids. Using a [3H]serine precursor and permeabilized yeast cells, it is possible to follow the synthesis of each of the aminoglycerophospholipids and examine the requirements for their interorganelle transport. This experimental approach reveals that in permeabilized cells newly synthesized phosphatidylserine is readily translocated to the locus of phosphatidylserine decarboxylase 1 in the mitochondria but not to the locus of phosphatidylserine decarboxylase 2 in the Golgi and vacuoles. Phosphatidylserine transport to the mitochondria is ATP independent and exhibits no requirements for cytosolic factors. The phosphatidylethanolamine formed in the mitochondria is exported to the locus of the methyltransferases (principally the endoplasmic reticulum) and converted to phosphatidylcholine. The export of phosphatidylethanolamine requires ATP but not any other cytosolic factors and is not obligately coupled to methyltransferase activity. The above described lipid transport reactions also occur in permeabilized cells that have been disrupted by homogenization, indicating that the processes are extremely efficient and may be dependent upon stable structural elements between organelles.
doi_str_mv 10.1074/jbc.270.50.29836
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purification</topic><topic>Phosphatidylcholines - metabolism</topic><topic>Phosphatidylethanolamines - biosynthesis</topic><topic>Phosphatidylethanolamines - isolation &amp; purification</topic><topic>Phosphatidylethanolamines - metabolism</topic><topic>Phosphatidylserines - biosynthesis</topic><topic>Phosphatidylserines - isolation &amp; purification</topic><topic>Phosphatidylserines - metabolism</topic><topic>Radioisotope Dilution Technique</topic><topic>RETICULO ENDOPLASMATICO</topic><topic>RETICULUM ENDOPLASMIQUE</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Serine - metabolism</topic><topic>Spheroplasts - metabolism</topic><topic>TRANSFERASAS</topic><topic>TRANSFERASE</topic><topic>Tritium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Achleitner, Georg</creatorcontrib><creatorcontrib>Zweytick, Dagmar</creatorcontrib><creatorcontrib>Trotter, Pamela J.</creatorcontrib><creatorcontrib>Voelker, Dennis R.</creatorcontrib><creatorcontrib>Daum, Günther</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Achleitner, Georg</au><au>Zweytick, Dagmar</au><au>Trotter, Pamela J.</au><au>Voelker, Dennis R.</au><au>Daum, Günther</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Synthesis and Intracellular Transport of Aminoglycerophospholipids in Permeabilized Cells of the Yeast, Saccharomyces cerevisiae(∗)</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1995-12-15</date><risdate>1995</risdate><volume>270</volume><issue>50</issue><spage>29836</spage><epage>29842</epage><pages>29836-29842</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The sequence of biosynthetic steps from phosphatidylserine to phosphatidylethanolamine (via decarboxylation) and then phosphatidylcholine (via methylation) is linked to the intracellular transport of these aminoglycerophospholipids. Using a [3H]serine precursor and permeabilized yeast cells, it is possible to follow the synthesis of each of the aminoglycerophospholipids and examine the requirements for their interorganelle transport. This experimental approach reveals that in permeabilized cells newly synthesized phosphatidylserine is readily translocated to the locus of phosphatidylserine decarboxylase 1 in the mitochondria but not to the locus of phosphatidylserine decarboxylase 2 in the Golgi and vacuoles. Phosphatidylserine transport to the mitochondria is ATP independent and exhibits no requirements for cytosolic factors. The phosphatidylethanolamine formed in the mitochondria is exported to the locus of the methyltransferases (principally the endoplasmic reticulum) and converted to phosphatidylcholine. The export of phosphatidylethanolamine requires ATP but not any other cytosolic factors and is not obligately coupled to methyltransferase activity. The above described lipid transport reactions also occur in permeabilized cells that have been disrupted by homogenization, indicating that the processes are extremely efficient and may be dependent upon stable structural elements between organelles.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8530379</pmid><doi>10.1074/jbc.270.50.29836</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record>
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subjects ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
BIOCHIMIE
Biological Transport
BIOQUIMICA
CEFALINAS
Cell Fractionation
Cell Membrane Permeability
CEPHALINE
Cytosol - metabolism
Kinetics
LECITHINE
LECITINAS
LIASAS
LIPOGENESE
LIPOGENESIS
LYASE
Methyltransferases - metabolism
Microsomes - metabolism
Mitochondria - metabolism
MITOCHONDRIE
MITOCONDRIA
ORGANITE CELLULAIRE
ORGANULOS CITOPLASMICOS
Phosphatidylcholines - biosynthesis
Phosphatidylcholines - isolation & purification
Phosphatidylcholines - metabolism
Phosphatidylethanolamines - biosynthesis
Phosphatidylethanolamines - isolation & purification
Phosphatidylethanolamines - metabolism
Phosphatidylserines - biosynthesis
Phosphatidylserines - isolation & purification
Phosphatidylserines - metabolism
Radioisotope Dilution Technique
RETICULO ENDOPLASMATICO
RETICULUM ENDOPLASMIQUE
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - metabolism
Serine - metabolism
Spheroplasts - metabolism
TRANSFERASAS
TRANSFERASE
Tritium
title Synthesis and Intracellular Transport of Aminoglycerophospholipids in Permeabilized Cells of the Yeast, Saccharomyces cerevisiae(∗)
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