Intrinsic unstructuredness and abundance of PEST motifs in eukaryotic proteomes
The study of unfolded protein regions has gained importance because of their prevalence and important roles in various cellular functions. These regions have characteristically high net charge and low hydrophobicity. The amino acid sequence determines the intrinsic unstructuredness of a region and,...
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| Published in | Proteins, structure, function, and bioinformatics Vol. 62; no. 2; pp. 309 - 315 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
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Wiley Subscription Services, Inc., A Wiley Company
01.02.2006
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| Abstract | The study of unfolded protein regions has gained importance because of their prevalence and important roles in various cellular functions. These regions have characteristically high net charge and low hydrophobicity. The amino acid sequence determines the intrinsic unstructuredness of a region and, therefore, efforts are ongoing to delineate the sequence motifs, which might contribute to protein disorder. We find that PEST motifs are enriched in the characterized disordered regions as compared with globular ones. Analysis of representative PDB chains revealed very few structures containing PEST sequences and the majority of them lacked regular secondary structure. A proteome‐wide study in completely sequenced eukaryotes with predicted unfolded and folded proteins shows that PEST proteins make up a large fraction of unfolded dataset as compared with the folded proteins. Our data also reveal the prevalence of PEST proteins in eukaryotic proteomes (∼25%). Functional classification of the PEST‐containing proteins shows an over‐ and under‐representation in proteins involved in regulation and metabolism, respectively. Furthermore, our analysis shows that predicted PEST regions do not exhibit any preference to be localized in the C terminals of proteins, as reported earlier. Proteins 2006. © 2005 Wiley‐Liss, Inc. |
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| AbstractList | The study of unfolded protein regions has gained importance because of their prevalence and important roles in various cellular functions. These regions have characteristically high net charge and low hydrophobicity. The amino acid sequence determines the intrinsic unstructuredness of a region and, therefore, efforts are ongoing to delineate the sequence motifs, which might contribute to protein disorder. We find that PEST motifs are enriched in the characterized disordered regions as compared with globular ones. Analysis of representative PDB chains revealed very few structures containing PEST sequences and the majority of them lacked regular secondary structure. A proteome-wide study in completely sequenced eukaryotes with predicted unfolded and folded proteins shows that PEST proteins make up a large fraction of unfolded dataset as compared with the folded proteins. Our data also reveal the prevalence of PEST proteins in eukaryotic proteomes (approximately 25%). Functional classification of the PEST-containing proteins shows an over- and under-representation in proteins involved in regulation and metabolism, respectively. Furthermore, our analysis shows that predicted PEST regions do not exhibit any preference to be localized in the C terminals of proteins, as reported earlier. Abstract The study of unfolded protein regions has gained importance because of their prevalence and important roles in various cellular functions. These regions have characteristically high net charge and low hydrophobicity. The amino acid sequence determines the intrinsic unstructuredness of a region and, therefore, efforts are ongoing to delineate the sequence motifs, which might contribute to protein disorder. We find that PEST motifs are enriched in the characterized disordered regions as compared with globular ones. Analysis of representative PDB chains revealed very few structures containing PEST sequences and the majority of them lacked regular secondary structure. A proteome‐wide study in completely sequenced eukaryotes with predicted unfolded and folded proteins shows that PEST proteins make up a large fraction of unfolded dataset as compared with the folded proteins. Our data also reveal the prevalence of PEST proteins in eukaryotic proteomes (∼25%). Functional classification of the PEST‐containing proteins shows an over‐ and under‐representation in proteins involved in regulation and metabolism, respectively. Furthermore, our analysis shows that predicted PEST regions do not exhibit any preference to be localized in the C terminals of proteins, as reported earlier. Proteins 2006. © 2005 Wiley‐Liss, Inc. The study of unfolded protein regions has gained importance because of their prevalence and important roles in various cellular functions. These regions have characteristically high net charge and low hydrophobicity. The amino acid sequence determines the intrinsic unstructuredness of a region and, therefore, efforts are ongoing to delineate the sequence motifs, which might contribute to protein disorder. We find that PEST motifs are enriched in the characterized disordered regions as compared with globular ones. Analysis of representative PDB chains revealed very few structures containing PEST sequences and the majority of them lacked regular secondary structure. A proteome‐wide study in completely sequenced eukaryotes with predicted unfolded and folded proteins shows that PEST proteins make up a large fraction of unfolded dataset as compared with the folded proteins. Our data also reveal the prevalence of PEST proteins in eukaryotic proteomes (∼25%). Functional classification of the PEST‐containing proteins shows an over‐ and under‐representation in proteins involved in regulation and metabolism, respectively. Furthermore, our analysis shows that predicted PEST regions do not exhibit any preference to be localized in the C terminals of proteins, as reported earlier. Proteins 2006. © 2005 Wiley‐Liss, Inc. |
| Author | Dash, Debasis Ganapathi, Mythily Singh, Gajinder Pal Sandhu, Kuljeet Singh |
| Author_xml | – sequence: 1 givenname: Gajinder Pal surname: Singh fullname: Singh, Gajinder Pal organization: Institute of Genomics and Integrative Biology (CSIR), Delhi University Campus, Delhi, India – sequence: 2 givenname: Mythily surname: Ganapathi fullname: Ganapathi, Mythily organization: Institute of Genomics and Integrative Biology (CSIR), Delhi University Campus, Delhi, India – sequence: 3 givenname: Kuljeet Singh surname: Sandhu fullname: Sandhu, Kuljeet Singh organization: Institute of Genomics and Integrative Biology (CSIR), Delhi University Campus, Delhi, India – sequence: 4 givenname: Debasis surname: Dash fullname: Dash, Debasis email: ddash@igib.res.in organization: Institute of Genomics and Integrative Biology (CSIR), Delhi University Campus, Delhi, India |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16299712$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Amino Acid Sequence Animals Genome Humans PEST motifs protein degradation signals Protein Denaturation protein disorder Protein Folding protein unfoldedness Proteins - chemistry Proteins - genetics proteolysis Proteome Surface Properties unstructured regions |
| Title | Intrinsic unstructuredness and abundance of PEST motifs in eukaryotic proteomes |
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