A common structural motif in nuclear pore proteins (nucleoporins)

BioEssays ◽  
1991 ◽  
Vol 13 (3) ◽  
pp. 145-146 ◽  
Author(s):  
Christopher M. Starr ◽  
John A. Hanover
Keyword(s):  
Structural Motif ◽  
Nuclear Pore ◽  
Nuclear Pore Proteins

scholarly journals Nuclear pore proteins are involved in the biogenesis of functional tRNA.

1996 ◽  
Vol 15 (9) ◽  
pp. 2270-2284 ◽  
Author(s):  
G. Simos ◽  
H. Tekotte ◽  
H. Grosjean ◽  
A. Segref ◽  
K. Sharma ◽  
...  
Keyword(s):  
Nuclear Pore ◽  
Nuclear Pore Proteins

scholarly journals Role of HSV-1 Capsid Vertex-Specific Component (CVSC) and Viral Terminal DNA in Capsid Docking at the Nuclear Pore

Viruses ◽  
2021 ◽  
Vol 13 (12) ◽  
pp. 2515
Author(s):  
José Ramon Villanueva-Valencia ◽  
Efthymios Tsimtsirakis ◽  
Alex Evilevitch
Keyword(s):  
Cell Nucleus ◽  
Experimental System ◽  
Structural Motif ◽  
Nuclear Pore ◽  
Structural Element ◽  
Viral Dna ◽  
Specific Component ◽  
Correct Orientation ◽  
Hsv 1

Penetration of the viral genome into a host cell nucleus is critical for initiation of viral replication for most DNA viruses and a few RNA viruses. For herpesviruses, viral DNA ejection into a nucleus occurs when the capsid docks at the nuclear pore complex (NPC) basket with the correct orientation of the unique capsid portal vertex. It has been shown that capsid vertex-specific component (CVSC) proteins, which are located at the twelve vertices of the human herpes simplex virus type 1 (HSV-1) capsid, interact with nucleoporins (Nups) of NPCs. However, it remained unclear whether CVSC proteins determine capsid-to-NPC binding. Furthermore, it has been speculated that terminal DNA adjacent to the portal complex of DNA-filled C-capsids forms a structural motif with the portal cap (which retains DNA in the capsid), which mediates capsid-NPC binding. We demonstrate that terminal viral DNA adjacent to the portal proteins does not present a structural element required for capsid-NPC binding. Our data also show that level of CVSC proteins on the HSV-1 capsid affects level of NPC binding. To elucidate the capsid-binding process, we use an isolated, reconstituted cell nucleus system that recapitulates capsid-nucleus binding in vivo without interference from trafficking kinetics of capsids moving toward the nucleus. This allows binding of non-infectious capsid maturation intermediates with varying levels of vertex-specific components. This experimental system provides a platform for investigating virus–host interaction at the nuclear membrane.

scholarly journals Nuclear Pore Proteins Nup153 and Megator Define Transcriptionally Active Regions in the Drosophila Genome

PLoS Genetics ◽  
2010 ◽  
Vol 6 (2) ◽  
pp. e1000846 ◽  
Author(s):  
Juan M. Vaquerizas ◽  
Ritsuko Suyama ◽  
Jop Kind ◽  
Kota Miura ◽  
Nicholas M. Luscombe ◽  
...  
Keyword(s):  
Active Regions ◽  
Nuclear Pore ◽  
Drosophila Genome ◽  
Nuclear Pore Proteins

scholarly journals The nuclear pore proteins Nup88/214 and T-cell acute lymphatic leukemia–associated NUP214 fusion proteins regulate Notch signaling

2019 ◽  
Vol 294 (31) ◽  
pp. 11741-11750 ◽  
Author(s):  
Bastian Kindermann ◽  
Christina Valkova ◽  
Andreas Krämer ◽  
Birgit Perner ◽  
Christian Engelmann ◽  
...  
Keyword(s):  
T Cell ◽  
Notch Signaling ◽  
Fusion Proteins ◽  
Nuclear Pore ◽  
Acute Lymphatic Leukemia ◽  
Lymphatic Leukemia ◽  
Nuclear Pore Proteins
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