scholarly journals Chromulinavorax destructans, a pathogenic TM6 bacterium with an unusual replication strategy targeting protist mitochondrion

2018 ◽  
Author(s):  
Christoph M. Deeg ◽  
Matthias M. Zimmer ◽  
Emma George ◽  
Filip Husnik ◽  
Patrick J. Keeling ◽  
...  

AbstractMost of the diversity of microbial life is not available in culture, and as such we lack even a fundamental understanding of the biological diversity of several branches on the tree of life. One branch that is highly underrepresented is the candidate phylum TM6, also known as the Dependentiae. Their biology is known only from reduced genomes recovered from metagenomes around the world and two isolates infecting amoebae, all suggest that they live highly host-associated lifestyles as parasites or symbionts.Chromulinavorax destructansis an isolate from the TM6/Dependentiae that infects and lyses the abundant heterotrophic flagellate,Spumella elongata. Chromulinavorax destructansis characterized by a high degree of reduction and specialization for infection, so much so it was discovered in a screen for giant viruses. Its 1.2 Mb genome shows no metabolic potential andC. destructansinstead relies on extensive transporter system to import nutrients, and even energy in the form of ATP from the host. Accordingly, it replicates in a viral-like fashion, while extensively reorganizing and expanding the host mitochondrion. 44% of proteins contain signal sequences for secretion, which includes many proteins of unknown function as well as 98 copies of ankyrin-repeat domain proteins, known effectors of host modulation, suggesting the presence of an extensive host-manipulation apparatus.

2007 ◽  
Vol 282 (33) ◽  
pp. 24027-24038 ◽  
Author(s):  
Mathew L. Coleman ◽  
Michael A. McDonough ◽  
Kirsty S. Hewitson ◽  
Charlotte Coles ◽  
Jasmin Mecinović ◽  
...  

2009 ◽  
Vol 1177 (1) ◽  
pp. 9-18 ◽  
Author(s):  
Matthew E. Cockman ◽  
James D. Webb ◽  
Peter J. Ratcliffe

2017 ◽  
Vol 45 (3) ◽  
pp. 741-750 ◽  
Author(s):  
Sjoerd J. van Deventer ◽  
Vera-Marie E. Dunlock ◽  
Annemiek B. van Spriel

To facilitate the myriad of different (signaling) processes that take place at the plasma membrane, cells depend on a high degree of membrane protein organization. Important mediators of this organization are tetraspanin proteins. Tetraspanins interact laterally among themselves and with partner proteins to control the spatial organization of membrane proteins in large networks called the tetraspanin web. The molecular interactions underlying the formation of the tetraspanin web were hitherto mainly described based on their resistance to different detergents, a classification which does not necessarily correlate with functionality in the living cell. To look at these interactions from a more physiological point of view, this review discusses tetraspanin interactions based on their function in the tetraspanin web: (1) intramolecular interactions supporting tetraspanin structure, (2) tetraspanin–tetraspanin interactions supporting web formation, (3) tetraspanin–partner interactions adding functional partners to the web and (4) cytosolic tetraspanin interactions regulating intracellular signaling. The recent publication of the first full-length tetraspanin crystal structure sheds new light on both the intra- and intermolecular tetraspanin interactions that shape the tetraspanin web. Furthermore, recent molecular dynamic modeling studies indicate that the binding strength between tetraspanins and between tetraspanins and their partners is the complex sum of both promiscuous and specific interactions. A deeper insight into this complex mixture of interactions is essential to our fundamental understanding of the tetraspanin web and its dynamics which constitute a basic building block of the cell surface.


2013 ◽  
Vol 32 (1) ◽  
pp. 35 ◽  
Author(s):  
Rui Bai ◽  
Dan Li ◽  
Zhong Shi ◽  
Xuefeng Fang ◽  
Weiting Ge ◽  
...  

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Akiko Takahashi ◽  
Masahiro Seike ◽  
Mika Chiba ◽  
Satoshi Takahashi ◽  
Shinji Nakamichi ◽  
...  

Cell Calcium ◽  
2020 ◽  
Vol 90 ◽  
pp. 102228 ◽  
Author(s):  
Lavanya Moparthi ◽  
Satish Babu Moparthi ◽  
Jérôme Wenger ◽  
Peter M. Zygmunt

2011 ◽  
Vol 108 (25) ◽  
pp. 10178-10183 ◽  
Author(s):  
J. A. Lamboy ◽  
H. Kim ◽  
K. S. Lee ◽  
T. Ha ◽  
E. A. Komives

Sign in / Sign up

Export Citation Format

Share Document