Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Tina Motwani"'
Autor:
Brianna M. Woodbury, Tina Motwani, Makayla N. Leroux, Lauren F. Barnes, Nicholas A. Lyktey, Sanchari Banerjee, Corynne L. Dedeo, Martin F. Jarrold, Carolyn M. Teschke
Publikováno v:
Viruses, Vol 14, Iss 7, p 1400 (2022)
The oligomerization and incorporation of the bacteriophage P22 portal protein complex into procapsids (PCs) depends upon an interaction with scaffolding protein, but the region of the portal protein that interacts with scaffolding protein has not bee
Externí odkaz:
https://doaj.org/article/e9045634e7dd4872a8e106b9a7a8c50f
Autor:
Ravi K. Lokareddy, Rajeshwer S. Sankhala, Ankoor Roy, Pavel V. Afonine, Tina Motwani, Carolyn M. Teschke, Kristin N. Parent, Gino Cingolani
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
Tailed bacteriophages assemble empty precursor capsids known as procapsids that are subsequently filled with viral DNA by a genome-packaging motor. Here the authors present a structure-based analysis that suggests the signal for termination of genome
Externí odkaz:
https://doaj.org/article/9153c6cc3a8e422c89bc78e6f3ac607c
Autor:
Weimin Wu, Justin C. Leavitt, Naiqian Cheng, Eddie B. Gilcrease, Tina Motwani, Carolyn M. Teschke, Sherwood R. Casjens, Alasdair C. Steven
Publikováno v:
mBio, Vol 7, Iss 4 (2016)
ABSTRACT The P22 capsid is a T=7 icosahedrally symmetric protein shell with a portal protein dodecamer at one 5-fold vertex. Extending outwards from that vertex is a short tail, and putatively extending inwards is a 15-nm-long α-helical barrel forme
Externí odkaz:
https://doaj.org/article/9b9b267307a1486f8926e69d4dbbe79f
Autor:
Tina Motwani, Carolyn M. Teschke
Publikováno v:
Journal of Virology. 93
Tailed double-stranded DNA (dsDNA) bacteriophages, herpesviruses, and adenoviruses package their genetic material into a precursor capsid through a dodecameric ring complex called the portal protein, which is located at a unique 5-fold vertex. In sev
Autor:
Carolyn M. Teschke, Tina Motwani, Juliana R. Cortines, Carmen A. Dunbar, Gino Cingolani, Martin F. Jarrold, Ravi K. Lokareddy
Publikováno v:
Science Advances
A novel role for scaffolding protein in portal ring formation.
Most double-stranded DNA viruses package genetic material into empty precursor capsids (or procapsids) through a dodecameric portal protein complex that occupies 1 of the 12 vertices
Most double-stranded DNA viruses package genetic material into empty precursor capsids (or procapsids) through a dodecameric portal protein complex that occupies 1 of the 12 vertices
Autor:
Tina Motwani, Pavel V. Afonine, Gino Cingolani, Kristin N. Parent, Ravi K. Lokareddy, Rajeshwer S. Sankhala, Ankoor Roy, Carolyn M. Teschke
Publikováno v:
Lokareddy, RK; Sankhala, RS; Roy, A; Afonine, PV; Motwani, T; Teschke, CM; et al.(2017). Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation. Nature Communications, 8. doi: 10.1038/ncomms14310. Lawrence Berkeley National Laboratory: Lawrence Berkeley National Laboratory. Retrieved from: http://www.escholarship.org/uc/item/1rn2d7s7
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
Nature communications, vol 8, iss 1
Nature Communications
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
Nature communications, vol 8, iss 1
Nature Communications
Tailed bacteriophages and herpesviruses assemble infectious particles via an empty precursor capsid (or ‘procapsid') built by multiple copies of coat and scaffolding protein and by one dodecameric portal protein. Genome packaging triggers rearrange
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2661e945d93a26a3dcba63019d09bb3b
http://www.escholarship.org/uc/item/1rn2d7s7
http://www.escholarship.org/uc/item/1rn2d7s7
Publikováno v:
Journal of Virology. 88:5287-5297
Icosahedral virus assembly requires a series of concerted and highly specific protein-protein interactions to produce a proper capsid. In bacteriophage P22, only coat protein (gp5) and scaffolding protein (gp8) are needed to assemble a procapsid-like
Autor:
Eddie B. Gilcrease, Carolyn M. Teschke, Justin C. Leavitt, Alasdair C. Steven, Tina Motwani, Naiqian Cheng, Sherwood R. Casjens, Weimin Wu
Publikováno v:
mBio
mBio, Vol 7, Iss 4 (2016)
mBio, Vol 7, Iss 4, p e01152-16 (2016)
mBio, Vol 7, Iss 4 (2016)
mBio, Vol 7, Iss 4, p e01152-16 (2016)
The P22 capsid is a T=7 icosahedrally symmetric protein shell with a portal protein dodecamer at one 5-fold vertex. Extending outwards from that vertex is a short tail, and putatively extending inwards is a 15-nm-long α-helical barrel formed by the
Autor:
Carolyn M. Teschke, Oghenefejiro Okifo, Andrei T. Alexandrescu, Christina Harprecht, Tina Motwani, Kevin J. Robbins
Publikováno v:
The Journal of biological chemistry. 291(21)
The I-domain is a genetic insertion in the phage P22 coat protein that chaperones its folding and stability. Of 11 acidic residues in the I-domain, seven participate in stabilizing electrostatic interactions with basic residues across elements of sec
Publikováno v:
Molecular and Cellular Biology. 32:2784-2793
Epigenetic mechanisms maintain the specific characteristics of differentiated cells by ensuring the inheritance of gene expression patterns through DNA replication and mitosis. We examined the mechanism of epigenetic inheritance of Sir protein-depend