Intermodular Communication in Polyketide Synthases: Comparing the Role of Protein−Protein Interactions to Those in Other Multidomain Proteins
Although the role of protein−protein interactions in transducing signals within biological systems has been extensively explored, their relevance to the channeling of intermediates in metabolism is not widely appreciated. Polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs) are t...
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Published in | Biochemistry (Easton) Vol. 40; no. 8; pp. 2317 - 2325 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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United States
American Chemical Society
27.02.2001
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Abstract | Although the role of protein−protein interactions in transducing signals within biological systems has been extensively explored, their relevance to the channeling of intermediates in metabolism is not widely appreciated. Polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs) are two related families of modular megasynthases that channel covalently bound intermediates from one active site to the next. Recent biochemical studies have highlighted the importance of protein−protein interactions in these chain transfer processes. The information available on this subject is reviewed, and its possible mechanistic implications are placed in context by comparisons with selected well-studied multicomponent protein systems. |
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AbstractList | Although the role of protein-protein interactions in transducing signals within biological systems has been extensively explored, their relevance to the channeling of intermediates in metabolism is not widely appreciated. Polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs) are two related families of modular megasynthases that channel covalently bound intermediates from one active site to the next. Recent biochemical studies have highlighted the importance of protein-protein interactions in these chain transfer processes. The information available on this subject is reviewed, and its possible mechanistic implications are placed in context by comparisons with selected well-studied multicomponent protein systems.Although the role of protein-protein interactions in transducing signals within biological systems has been extensively explored, their relevance to the channeling of intermediates in metabolism is not widely appreciated. Polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs) are two related families of modular megasynthases that channel covalently bound intermediates from one active site to the next. Recent biochemical studies have highlighted the importance of protein-protein interactions in these chain transfer processes. The information available on this subject is reviewed, and its possible mechanistic implications are placed in context by comparisons with selected well-studied multicomponent protein systems. Although the role of protein−protein interactions in transducing signals within biological systems has been extensively explored, their relevance to the channeling of intermediates in metabolism is not widely appreciated. Polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs) are two related families of modular megasynthases that channel covalently bound intermediates from one active site to the next. Recent biochemical studies have highlighted the importance of protein−protein interactions in these chain transfer processes. The information available on this subject is reviewed, and its possible mechanistic implications are placed in context by comparisons with selected well-studied multicomponent protein systems. Although the role of protein-protein interactions in transducing signals within biological systems has been extensively explored, their relevance to the channeling of intermediates in metabolism is not widely appreciated. Polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs) are two related families of modular megasynthases that channel covalently bound intermediates from one active site to the next. Recent biochemical studies have highlighted the importance of protein-protein interactions in these chain transfer processes. The information available on this subject is reviewed, and its possible mechanistic implications are placed in context by comparisons with selected well-studied multicomponent protein systems. |
Author | Wu, Nicholas Tsuji, Stuart Y Khosla, Chaitan |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/11327851$$D View this record in MEDLINE/PubMed |
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Notes | Research in the authors' laboratory on modular PKSs has been supported by grants from the National Institutes of Health (1 R01-CA66736), the National Science Foundation (BES 9806774), and the Strategic Research Fund of AstraZeneca, Inc. S.Y.T. is a recipient of an NSF Predoctoral Fellowship, and N.W. is a recipient of a Stanford−NIH Predoctoral Training Fellowship. istex:AAF3D6016E3C7D9AA5F5EA7C936DF7C2B9065CD6 ark:/67375/TPS-BDVKPDM3-5 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 ObjectType-Review-3 content type line 23 |
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SubjectTerms | 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase - chemistry 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase - metabolism Animals Humans Multienzyme Complexes - chemistry Multienzyme Complexes - metabolism Protein Structure, Tertiary Proteins - chemistry Proteins - metabolism Proto-Oncogene Proteins c-fos - chemistry Proto-Oncogene Proteins c-fos - metabolism Proto-Oncogene Proteins c-jun - chemistry Proto-Oncogene Proteins c-jun - metabolism Pyruvate Dehydrogenase Complex - chemistry Pyruvate Dehydrogenase Complex - metabolism src-Family Kinases - chemistry src-Family Kinases - metabolism |
Title | Intermodular Communication in Polyketide Synthases: Comparing the Role of Protein−Protein Interactions to Those in Other Multidomain Proteins |
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