Novel peroxisome clustering mutants and peroxisome biogenesis mutants of Saccharomyces cerevisiae

The goal of this research is to identify and characterize the protein machinery that functions in the intracellular translocation and assembly of peroxisomal proteins in Saccharomyces cerevisiae. Several genes encoding proteins that are essential for this process have been identified previously by K...

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Veröffentlicht in:The Journal of cell biology 1993-12, Vol.123 (5), p.1133-1147
Hauptverfasser: Zhang, J.W, Han, Y, Lazarow, P.B
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creator Zhang, J.W
Han, Y
Lazarow, P.B
description The goal of this research is to identify and characterize the protein machinery that functions in the intracellular translocation and assembly of peroxisomal proteins in Saccharomyces cerevisiae. Several genes encoding proteins that are essential for this process have been identified previously by Kunau and collaborators, but the mutant collection was incomplete. We have devised a positive selection procedure that identifies new mutants lacking peroxisomes or peroxisomal function. Immunofluorescence procedures for yeast were simplified so that these mutants could be rapidly and efficiently screened for those in which peroxisome biogenesis is impaired. With these tools, we have identified four complementation groups of peroxisome biogenesis mutants, and one group that appears to express reduced amounts of peroxisomal proteins. Two of our mutants lack recognizable peroxisomes, although they might contain peroxisomal membrane ghosts like those found in Zellweger syndrome. Two are selectively defective in packaging peroxisomal proteins and moreover show striking intracellular clustering of the peroxisomes. The distribution of mutants among complementation groups implies that the collection of peroxisome biogenesis mutants is still incomplete. With the procedures described, it should prove straightforward to isolate mutants from additional complementation groups
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Several genes encoding proteins that are essential for this process have been identified previously by Kunau and collaborators, but the mutant collection was incomplete. We have devised a positive selection procedure that identifies new mutants lacking peroxisomes or peroxisomal function. Immunofluorescence procedures for yeast were simplified so that these mutants could be rapidly and efficiently screened for those in which peroxisome biogenesis is impaired. With these tools, we have identified four complementation groups of peroxisome biogenesis mutants, and one group that appears to express reduced amounts of peroxisomal proteins. Two of our mutants lack recognizable peroxisomes, although they might contain peroxisomal membrane ghosts like those found in Zellweger syndrome. Two are selectively defective in packaging peroxisomal proteins and moreover show striking intracellular clustering of the peroxisomes. The distribution of mutants among complementation groups implies that the collection of peroxisome biogenesis mutants is still incomplete. 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Several genes encoding proteins that are essential for this process have been identified previously by Kunau and collaborators, but the mutant collection was incomplete. We have devised a positive selection procedure that identifies new mutants lacking peroxisomes or peroxisomal function. Immunofluorescence procedures for yeast were simplified so that these mutants could be rapidly and efficiently screened for those in which peroxisome biogenesis is impaired. With these tools, we have identified four complementation groups of peroxisome biogenesis mutants, and one group that appears to express reduced amounts of peroxisomal proteins. Two of our mutants lack recognizable peroxisomes, although they might contain peroxisomal membrane ghosts like those found in Zellweger syndrome. Two are selectively defective in packaging peroxisomal proteins and moreover show striking intracellular clustering of the peroxisomes. The distribution of mutants among complementation groups implies that the collection of peroxisome biogenesis mutants is still incomplete. With the procedures described, it should prove straightforward to isolate mutants from additional complementation groups</description><subject>Acetyl-CoA C-Acetyltransferase - isolation &amp; purification</subject><subject>Acetyl-CoA C-Acetyltransferase - metabolism</subject><subject>Antibodies</subject><subject>Biological and medical sciences</subject><subject>Biological Transport</subject><subject>Catalase - isolation &amp; purification</subject><subject>Catalase - metabolism</subject><subject>Cell biology</subject><subject>Cell metabolism, cell oxidation</subject><subject>Cell physiology</subject><subject>Cells</subject><subject>Cellular biology</subject><subject>Clone Cells</subject><subject>Complementation</subject><subject>Crosses, Genetic</subject><subject>Enzymes</subject><subject>Fatty acids</subject><subject>Fluorescence</subject><subject>Fluorescent Antibody Technique</subject><subject>Fluorescent antibody techniques</subject><subject>Fundamental and applied biological sciences. 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Several genes encoding proteins that are essential for this process have been identified previously by Kunau and collaborators, but the mutant collection was incomplete. We have devised a positive selection procedure that identifies new mutants lacking peroxisomes or peroxisomal function. Immunofluorescence procedures for yeast were simplified so that these mutants could be rapidly and efficiently screened for those in which peroxisome biogenesis is impaired. With these tools, we have identified four complementation groups of peroxisome biogenesis mutants, and one group that appears to express reduced amounts of peroxisomal proteins. Two of our mutants lack recognizable peroxisomes, although they might contain peroxisomal membrane ghosts like those found in Zellweger syndrome. Two are selectively defective in packaging peroxisomal proteins and moreover show striking intracellular clustering of the peroxisomes. The distribution of mutants among complementation groups implies that the collection of peroxisome biogenesis mutants is still incomplete. With the procedures described, it should prove straightforward to isolate mutants from additional complementation groups</abstract><cop>New York, NY</cop><pub>Rockefeller University Press</pub><pmid>7902359</pmid><doi>10.1083/jcb.123.5.1133</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record>
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subjects Acetyl-CoA C-Acetyltransferase - isolation & purification
Acetyl-CoA C-Acetyltransferase - metabolism
Antibodies
Biological and medical sciences
Biological Transport
Catalase - isolation & purification
Catalase - metabolism
Cell biology
Cell metabolism, cell oxidation
Cell physiology
Cells
Cellular biology
Clone Cells
Complementation
Crosses, Genetic
Enzymes
Fatty acids
Fluorescence
Fluorescent Antibody Technique
Fluorescent antibody techniques
Fundamental and applied biological sciences. Psychology
Fungal Proteins - metabolism
Genetic Complementation Test
GENETICA
GENETIQUE
Hydrogen Peroxide - pharmacology
IMMUNOFLUORESCENCE
INMUNOFLUORESCENCIA
Microbodies - metabolism
Microbodies - ultrastructure
Microscopy, Immunoelectron
Molecular and cellular biology
MUTANT
MUTANTES
Mutation
Oleic Acid
Oleic Acids - metabolism
Peroxisomes
PROTEINAS
PROTEINE
Proteins
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - drug effects
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae - ultrastructure
Selection, Genetic
Yeast
Yeasts
title Novel peroxisome clustering mutants and peroxisome biogenesis mutants of Saccharomyces cerevisiae
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