2006
DOI: 10.1073/pnas.0508409103
|View full text |Cite
|
Sign up to set email alerts
|

Harnessing the potential of communication-mediating domains for the biocombinatorial synthesis of nonribosomal peptides

Abstract: The interaction between enzymes of a nonribosomal peptide synthetase (NRPS) complex relies on the interplay of compatible sets of donor and acceptor communication-mediating (COM) domains. Hence, these domains are essential for the formation of a defined biosynthetic template, thereby directing the synthesis of a specific peptide product. Without the selectivity provided by different sets of COM domains, NRPSs should form random biosynthetic templates, which would ultimately lead to combinatorial peptide synthe… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1

Citation Types

2
104
0
5

Year Published

2008
2008
2020
2020

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 104 publications
(111 citation statements)
references
References 15 publications
2
104
0
5
Order By: Relevance
“…This strongly suggests the N terminus of ZmA initially contained a fatty acid, along with D-Asn. Finally, Chiocchini and colleagues and Hahn and Stachelhaus have shown that E domains and C domains that interact with each other contain communication domains that function as sites of specific protein-protein interactions between E and C domains on different NRPS polypeptides (7,15,16). Analysis of the C terminus of the E domain of ZmaO and the N terminus of ZmaK identified sequences consistent with communication domains (data not shown).…”
Section: Resultsmentioning
confidence: 95%
“…This strongly suggests the N terminus of ZmA initially contained a fatty acid, along with D-Asn. Finally, Chiocchini and colleagues and Hahn and Stachelhaus have shown that E domains and C domains that interact with each other contain communication domains that function as sites of specific protein-protein interactions between E and C domains on different NRPS polypeptides (7,15,16). Analysis of the C terminus of the E domain of ZmaO and the N terminus of ZmaK identified sequences consistent with communication domains (data not shown).…”
Section: Resultsmentioning
confidence: 95%
“…To this end, modern genetic techniques allow catalytic sites to be brought into close proximity in several ways. For example, enzymes may be engineered to assemble on supports via docking domains (10,13) or may be brought to interact via specific communication domains (15). However, the most simple and most studied approach is to simply fuse two open reading frames (ORFs) which encode different enzymatic activities.…”
mentioning
confidence: 99%
“…Another interpretation of these results is that, because of the missing N terminus of PhsA, an interaction between the N terminus of PhsA and the C terminus of PhsB or PhsC is not possible. As mentioned above, the N and C termini of the peptide synthetase play an essential role for the selective interaction and communication between peptide synthetases mediated by COM domains (14,15). Although no COM domains were identified in the PTT peptide synthetases (37), it cannot be excluded that there are specific sequences that exhibit the function of a COM domain and thus are responsible for the selective interaction of PhsA, PhsB, and PhsC.…”
Section: Discussionmentioning
confidence: 96%
“…The COM domains are classified into the accepter COM domain (COM A ) and the donor COM domain (COM D ). At the N terminus of the initiation module and at the C terminus of the termination module, a COM domain usually is lacking (14,15,26). However, in the PTT synthetases PhsA, PhsB, and PhsC, such COM domains are not apparent (37).…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation