Protein–protein interactions in trans-AT polyketide synthases

2018 ◽  
Vol 35 (10) ◽  
pp. 1097-1109 ◽  
Author(s):  
Simone Kosol ◽  
Matthew Jenner ◽  
Józef R. Lewandowski ◽  
Gregory L. Challis
Keyword(s):  
Protein Interactions ◽  
Polyketide Synthases ◽  
Protein Protein Interactions ◽  
Subunit Protein ◽  
In Trans

An extensive and highly programmed set of inter- and intra-subunit protein–protein interactions controls chain assembly by trans-AT polyketide synthases.

scholarly journals Engineering strategies for rational polyketide synthase design

2018 ◽  
Vol 35 (10) ◽  
pp. 1070-1081 ◽  
Author(s):  
Maja Klaus ◽  
Martin Grininger
Keyword(s):  
Protein Interactions ◽  
Assembly Line ◽  
Polyketide Synthase ◽  
Polyketide Synthases ◽  
Protein Protein Interactions ◽  
Important Protein ◽  
Line P

In this review, we highlight strategies in engineering polyketide synthases (PKSs). We focus on important protein–protein interactions that constitute an intact PKS assembly line.

scholarly journals Protein–protein interactions in “cis-AT” polyketide synthases

2018 ◽  
Vol 35 (10) ◽  
pp. 1082-1096 ◽  
Author(s):  
Greg J. Dodge ◽  
Finn P. Maloney ◽  
Janet L. Smith
Keyword(s):  
Protein Interactions ◽  
Active Site ◽  
Catalytic Domain ◽  
Polyketide Synthases ◽  
Protein Protein Interactions ◽  
P Protein ◽  
In Cis

Protein–protein interactions of cis-AT polyketide synthases are dominated by the travels of the ACP domain to the active site entrance of each catalytic domain.

scholarly journals Crystal structure of the glutamate receptor GluA1 N-terminal domain

2011 ◽  
Vol 438 (2) ◽  
pp. 255-263 ◽  
Author(s):  
Guorui Yao ◽  
Yinong Zong ◽  
Shenyan Gu ◽  
Jie Zhou ◽  
Huaxi Xu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Protein Interactions ◽  
Ampa Receptors ◽  
Neurological Diseases ◽  
Protein Protein Interactions ◽  
Terminal Domain ◽  
The Central Nervous System ◽  
In Trans ◽  
Excitatory Neurotransmission ◽  
Active Channels

The AMPA (α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid) subfamily of iGluRs (ionotropic glutamate receptors) is essential for fast excitatory neurotransmission in the central nervous system. The malfunction of AMPARs (AMPA receptors) has been implicated in many neurological diseases, including Alzheimer's disease, Parkinson's disease and amyotrophic lateral sclerosis. The active channels of AMPARs and other iGluR subfamilies are tetramers formed exclusively by assembly of subunits within the same subfamily. It has been proposed that the assembly process is controlled mainly by the extracellular ATD (N-terminal domain) of iGluR. In addition, ATD has also been implicated in synaptogenesis, iGluR trafficking and trans-synaptic signalling, through unknown mechanisms. We report in the present study a 2.5 Å (1 Å=0.1 nm) resolution crystal structure of the ATD of GluA1. Comparative analyses of the structure of GluA1-ATD and other subunits sheds light on our understanding of how ATD drives subfamily-specific assembly of AMPARs. In addition, analysis of the crystal lattice of GluA1-ATD suggests a novel mechanism by which the ATD might participate in inter-tetramer AMPAR clustering, as well as in trans-synaptic protein–protein interactions.

scholarly journals Protein-Protein Interactions, Not Substrate Recognition, Dominate the Turnover of Chimeric Assembly Line Polyketide Synthases

2016 ◽  
Vol 291 (31) ◽  
pp. 16404-16415 ◽  
Author(s):  
Maja Klaus ◽  
Matthew P. Ostrowski ◽  
Jonas Austerjost ◽  
Thomas Robbins ◽  
Brian Lowry ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Assembly Line ◽  
Substrate Recognition ◽  
Polyketide Synthases ◽  
Protein Protein Interactions

scholarly journals Coevolution-based prediction of protein-protein interactions in polyketide biosynthetic assembly lines

2019 ◽  
Author(s):  
Yan Wang ◽  
Miguel Correa Marrero ◽  
Marnix H. Medema ◽  
Aalt D.J. van Dijk
Keyword(s):  
Protein Interactions ◽  
Antitumor Agents ◽  
Acyl Carrier Protein ◽  
Specific Protein ◽  
Polyketide Synthases ◽  
Combinatorial Biosynthesis ◽  
Prediction Algorithm ◽  
Type I ◽  
Protein Protein Interactions ◽  
Assembly Lines

AbstractPolyketide synthases are multimodular enzymes that generate diverse molecules of great pharmaceutical importance, including a range of clinically used antimicrobials and antitumor agents. Many polyketides are synthesized by type I polyketide synthases (PKSs), which are organized in assembly lines, in which multiple enzymes line up in a specific order. This order is defined by specific protein-protein interactions. The unique modular structure and catalyzing mechanism of these assembly lines makes their products predictable and also spurred combinatorial biosynthesis studies to produce novel polyketides using synthetic biology. However, predicting the interactions of PKSs, and thereby inferring the order of their assembly line, is still challenging, especially for cases in which this order is not reflected by the ordering of the PKS-encoding genes in the genome. Here, we introduce PKSpop, which uses a coevolution-based protein-protein interaction prediction algorithm to infer protein order in PKS assembly lines. Our method accurately predicts protein orders (80% accuracy). Additionally, we identify new residue pairs that are key in determining interaction specificity, and show that coevolution of N- and C-terminal docking domains of PKSs is significantly more predictive for protein-protein interactions than coevolution between ketosynthase and acyl carrier protein domains.

Protein-protein interactions of the p53 family with the Bcl-2 family in hepatocellular carcinoma

2011 ◽  
Vol 49 (08) ◽  
Author(s):  
LC König ◽  
M Meinhard ◽  
C Sandig ◽  
MH Bender ◽  
A Lovas ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
P53 Family
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