scholarly journals Molecular Evolution of Cadherin-Related Neuronal Receptor/Protocadherin α (CNR/Pcdhα) Gene Cluster in Mus musculus Subspecies

2005 ◽  
Vol 22 (6) ◽  
pp. 1433-1443 ◽  
Author(s):  
Yusuke Taguchi ◽  
Tsuyoshi Koide ◽  
Toshihiko Shiroishi ◽  
Takeshi Yagi
BMC Genomics ◽  
2011 ◽  
Vol 12 (1) ◽  
Author(s):  
Alessandra F Ribas ◽  
Alberto Cenci ◽  
Marie-Christine Combes ◽  
Hervé Etienne ◽  
Philippe Lashermes

1992 ◽  
Vol 2 (1) ◽  
pp. 31-36 ◽  
Author(s):  
Sunil K. Ahuja ◽  
Tayfun Özçelik ◽  
Athena Milatovitch ◽  
Uta Francke ◽  
Philip M. Murphy

2011 ◽  
Vol 11 (1) ◽  
Author(s):  
Emiliano Mancini ◽  
Federica Tammaro ◽  
Francesco Baldini ◽  
Allegra Via ◽  
Domenico Raimondo ◽  
...  

1998 ◽  
Vol 46 (5) ◽  
pp. 589-601 ◽  
Author(s):  
Thomas Hankeln ◽  
Clara Amid ◽  
Bettina Weich ◽  
Jürgen Niessing ◽  
Erwin R. Schmidt

2017 ◽  
Vol 114 (24) ◽  
pp. E4822-E4831 ◽  
Author(s):  
Simon Schäper ◽  
Wieland Steinchen ◽  
Elizaveta Krol ◽  
Florian Altegoer ◽  
Dorota Skotnicka ◽  
...  

Cyclic dimeric GMP (c-di-GMP) has emerged as a key regulatory player in the transition between planktonic and sedentary biofilm-associated bacterial lifestyles. It controls a multitude of processes including production of extracellular polysaccharides (EPSs). The PilZ domain, consisting of an N-terminal “RxxxR” motif and a β-barrel domain, represents a prototype c-di-GMP receptor. We identified a class of c-di-GMP–responsive proteins, represented by the AraC-like transcription factor CuxR in plant symbiotic α-proteobacteria. In Sinorhizobium meliloti, CuxR stimulates transcription of an EPS biosynthesis gene cluster at elevated c-di-GMP levels. CuxR consists of a Cupin domain, a helical hairpin, and bipartite helix-turn-helix motif. Although unrelated in sequence, the mode of c-di-GMP binding to CuxR is highly reminiscent to that of PilZ domains. c-di-GMP interacts with a conserved N-terminal RxxxR motif and the Cupin domain, thereby promoting CuxR dimerization and DNA binding. We unravel structure and mechanism of a previously unrecognized c-di-GMP–responsive transcription factor and provide insights into the molecular evolution of c-di-GMP binding to proteins.


2020 ◽  
Vol 20 (1) ◽  
Author(s):  
Miriam Linnenbrink ◽  
Kristian K. Ullrich ◽  
Ellen McConnell ◽  
Diethard Tautz

Abstract Background Amylase gene clusters have been implicated in adaptive copy number changes in response to the amount of starch in the diet of humans and mammals. However, this interpretation has been questioned for humans and for mammals there is a paucity of information from natural populations. Results Using optical mapping and genome read information, we show here that the amylase cluster in natural house mouse populations is indeed copy-number variable for Amy2b paralogous gene copies (called Amy2a1 - Amy2a5), but a direct connection to starch diet is not evident. However, we find that the amylase cluster was subject to introgression of haplotypes between Mus musculus sub-species. A very recent introgression can be traced in the Western European populations and this leads also to the rescue of an Amy2b pseudogene. Some populations and inbred lines derived from the Western house mouse (Mus musculus domesticus) harbor a copy of the pancreatic amylase (Amy2b) with a stop codon in the first exon, making it non-functional. But populations in France harbor a haplotype introgressed from the Eastern house mouse (M. m. musculus) with an intact reading frame. Detailed analysis of phylogenetic patterns along the amylase cluster suggest an additional history of previous introgressions. Conclusions Our results show that the amylase gene cluster is a hotspot of introgression in the mouse genome, making it an evolutionary active region beyond the previously observed copy number changes.


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