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GPMDB Submission: Protein complexes in Saccharomyces cerevisiae

ABSTRACT: Not available

INSTRUMENT(S): instrument model

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Ronald Beavis

PROVIDER: PRD000006 | Pride | 2010-01-06

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	PRIDE_Exp_Complete_Ac_1000.pride.mztab.gz	Mztab
	PRIDE_Exp_Complete_Ac_1000.xml.gz	Xml
	PRIDE_Exp_Complete_Ac_1001.pride.mztab.gz	Mztab
	PRIDE_Exp_Complete_Ac_1001.xml.gz	Xml
	PRIDE_Exp_Complete_Ac_1002.pride.mztab.gz	Mztab

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Project description:Many successful functional studies by gene expression profiling in the literature have led to the perception that profile similarity is likely to imply functional association. But how true is the converse of the above statement? Do functionally associated genes tend to be co-regulated at the transcription level? In this paper, we focus on a set of well-validated yeast protein complexes provided by Munich Information Center for Protein Sequences (MIPS). Using four well-known large-scale microarray expression data sets, we computed the correlations between genes from the same complex. We then analyzed the relationship between the distribution of correlations and the complex size (the number of genes in a protein complex). We found that except for a few large protein complexes, such as mitochondrial ribosomal and cytoplasmic ribosomal proteins, the correlations are on the average not much higher than that from a pair of randomly selected genes. The global impact of large complexes on the expression of other genes in the genome is also studied. Our result also showed that the expression of over 85% of the genes are affected by six large complexes: the cytoplasmic ribosomal complex, mitochondrial ribosomal complex, proteasome complex, F0/F1 ATP synthase (complex V) (size 18), rRNA splicing (size 24) and H+- transporting ATPase, vacular (size 15).

| S-EPMC2632914 | biostudies-literature

Blue native electrophoresis combined with stable isotope labeling shows that Saccharomyces cerevisiae mitochondrial respiratory chain supercomplexes are still present under anaerobic conditions

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