Synthetic protein scaffolds based on peptide motifs and cognate adaptor domains for improving metabolic productivity
The efficiency of many cellular processes relies on the defined interaction among different proteins within the same metabolic or signaling pathway. Consequently, a spatial colocalization of functionally interacting proteins has frequently emerged during evolution. This concept has been adapted with...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2015-11-01
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| Series: | Frontiers in Bioengineering and Biotechnology |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fbioe.2015.00191/full |
| _version_ | 1818345834332291072 |
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| author | Anselm H.C. Horn Heinrich eSticht |
| author_facet | Anselm H.C. Horn Heinrich eSticht |
| author_sort | Anselm H.C. Horn |
| collection | DOAJ |
| description | The efficiency of many cellular processes relies on the defined interaction among different proteins within the same metabolic or signaling pathway. Consequently, a spatial colocalization of functionally interacting proteins has frequently emerged during evolution. This concept has been adapted within the synthetic biology community for the purpose of creating artificial scaffolds. A recent advancement of this concept is the use of peptide motifs and their cognate adaptor domains. SH2, SH3, GBD, and PDZ domains have been used most often in research studies to date. The approach has been successfully applied to the synthesis of a variety of target molecules including catechin, D-glucaric acid, H2, hydrochinone, resveratrol, butyrate, gamma-aminobutyric acid, and mevalonate. Increased production levels of up to 77-fold have been observed compared to non-scaffolded systems. A recent extension of this concept is the creation of a covalent linkage between peptide motifs and adaptor domains, which leads to a more stable association of the scaffolded systems and thus bears the potential to further enhance metabolic productivity. |
| first_indexed | 2024-12-13T17:08:40Z |
| format | Article |
| id | doaj.art-36104adc17434754a734c709671f115e |
| institution | Directory Open Access Journal |
| issn | 2296-4185 |
| language | English |
| last_indexed | 2024-12-13T17:08:40Z |
| publishDate | 2015-11-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Bioengineering and Biotechnology |
| spelling | doaj.art-36104adc17434754a734c709671f115e2022-12-21T23:37:36ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852015-11-01310.3389/fbioe.2015.00191166286Synthetic protein scaffolds based on peptide motifs and cognate adaptor domains for improving metabolic productivityAnselm H.C. Horn0Heinrich eSticht1University Erlangen-NurembergUniversity Erlangen-NurembergThe efficiency of many cellular processes relies on the defined interaction among different proteins within the same metabolic or signaling pathway. Consequently, a spatial colocalization of functionally interacting proteins has frequently emerged during evolution. This concept has been adapted within the synthetic biology community for the purpose of creating artificial scaffolds. A recent advancement of this concept is the use of peptide motifs and their cognate adaptor domains. SH2, SH3, GBD, and PDZ domains have been used most often in research studies to date. The approach has been successfully applied to the synthesis of a variety of target molecules including catechin, D-glucaric acid, H2, hydrochinone, resveratrol, butyrate, gamma-aminobutyric acid, and mevalonate. Increased production levels of up to 77-fold have been observed compared to non-scaffolded systems. A recent extension of this concept is the creation of a covalent linkage between peptide motifs and adaptor domains, which leads to a more stable association of the scaffolded systems and thus bears the potential to further enhance metabolic productivity.http://journal.frontiersin.org/Journal/10.3389/fbioe.2015.00191/fullMetabolic Engineeringfusion proteinProtein scaffoldadaptor domainlinear peptide motif |
| spellingShingle | Anselm H.C. Horn Heinrich eSticht Synthetic protein scaffolds based on peptide motifs and cognate adaptor domains for improving metabolic productivity Frontiers in Bioengineering and Biotechnology Metabolic Engineering fusion protein Protein scaffold adaptor domain linear peptide motif |
| title | Synthetic protein scaffolds based on peptide motifs and cognate adaptor domains for improving metabolic productivity |
| title_full | Synthetic protein scaffolds based on peptide motifs and cognate adaptor domains for improving metabolic productivity |
| title_fullStr | Synthetic protein scaffolds based on peptide motifs and cognate adaptor domains for improving metabolic productivity |
| title_full_unstemmed | Synthetic protein scaffolds based on peptide motifs and cognate adaptor domains for improving metabolic productivity |
| title_short | Synthetic protein scaffolds based on peptide motifs and cognate adaptor domains for improving metabolic productivity |
| title_sort | synthetic protein scaffolds based on peptide motifs and cognate adaptor domains for improving metabolic productivity |
| topic | Metabolic Engineering fusion protein Protein scaffold adaptor domain linear peptide motif |
| url | http://journal.frontiersin.org/Journal/10.3389/fbioe.2015.00191/full |
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