scholarly journals Lean forward: Genetic analysis of temperature-sensitive mutants unfolds the secrets of oligomeric protein complex assembly

BioEssays ◽  
2014 ◽  
Vol 36 (9) ◽  
pp. 836-846 ◽  
Author(s):  
Michael McMurray
Keyword(s):  
Genetic Analysis ◽  
Protein Complex ◽  
Temperature Sensitive ◽  
Complex Assembly ◽  
Temperature Sensitive Mutants ◽  
Oligomeric Protein ◽  
Protein Complex Assembly

scholarly journals Visualizing the Dynamics of Dystrophin Protein Complex Assembly in Living Cells

2005 ◽  
Vol 11 (S02) ◽  
Author(s):  
R A Draviam ◽  
B Wang ◽  
S Shand ◽  
X Xiao ◽  
S C Watkins
Keyword(s):  
Protein Complex ◽  
Living Cells ◽  
Complex Assembly ◽  
Dystrophin Protein ◽  
Protein Complex Assembly

Isolation and Genetic Analysis of Temperature-Sensitive Mutants of Rhinovirus Type 2

Intervirology ◽  
1980 ◽  
Vol 13 (5) ◽  
pp. 299-306 ◽  
Author(s):  
Martin R. Evans ◽  
John H. Hughes ◽  
Cicek Gercel ◽  
Vincent V. Hamparian
Keyword(s):  
Genetic Analysis ◽  
Temperature Sensitive ◽  
Temperature Sensitive Mutants

scholarly journals Retinal Cone Photoreceptors Require Phosducin-Like Protein 1 for G Protein Complex Assembly and Signaling

PLoS ONE ◽  
2015 ◽  
Vol 10 (2) ◽  
pp. e0117129 ◽  
Author(s):  
Christopher M. Tracy ◽  
Alexander V. Kolesnikov ◽  
Devon R. Blake ◽  
Ching-Kang Chen ◽  
Wolfgang Baehr ◽  
...  
Keyword(s):  
G Protein ◽  
Protein Complex ◽  
Cone Photoreceptors ◽  
Complex Assembly ◽  
Retinal Cone ◽  
Protein Complex Assembly

Genetic analysis of temperature-sensitive mutants of HSV-1: The combined use of complementation and physical mapping for cistron assignment

Virology ◽  
1983 ◽  
Vol 130 (2) ◽  
pp. 290-305 ◽  
Author(s):  
Sandra K. Weller ◽  
Doris P. Aschman ◽  
Wendy R. Sacks ◽  
Donald M. Coen ◽  
Priscilla A. Schaffer
Keyword(s):  
Genetic Analysis ◽  
Physical Mapping ◽  
Temperature Sensitive ◽  
Temperature Sensitive Mutants ◽  
Combined Use ◽  
Hsv 1

scholarly journals Complex formation by the Drosophila MSL proteins: role of the MSL2 RING finger in protein complex assembly

1998 ◽  
Vol 17 (18) ◽  
pp. 5409-5417 ◽  
Author(s):  
Kyle Copps ◽  
Ron Richman ◽  
Laura M. Lyman ◽  
Kimberly A. Chang ◽  
Joanne Rampersad-Ammons ◽  
...  
Keyword(s):  
Complex Formation ◽  
Protein Complex ◽  
Ring Finger ◽  
Complex Assembly ◽  
Protein Complex Assembly

scholarly journals Vac14 Protein Multimerization Is a Prerequisite Step for Fab1 Protein Complex Assembly and Function

2013 ◽  
Vol 288 (13) ◽  
pp. 9363-9372 ◽  
Author(s):  
Tamadher A. Alghamdi ◽  
Cheuk Y. Ho ◽  
Amra Mrakovic ◽  
Danielle Taylor ◽  
Daniel Mao ◽  
...  
Keyword(s):  
Protein Complex ◽  
Complex Assembly ◽  
Protein Multimerization ◽  
And Function ◽  
Protein Complex Assembly

scholarly journals Operon Gene Order Is Optimized for Ordered Protein Complex Assembly

Cell Reports ◽  
2016 ◽  
Vol 14 (4) ◽  
pp. 679-685 ◽  
Author(s):  
Jonathan N. Wells ◽  
L. Therese Bergendahl ◽  
Joseph A. Marsh
Keyword(s):  
Gene Order ◽  
Protein Complex ◽  
Complex Assembly ◽  
Operon Gene ◽  
Protein Complex Assembly

scholarly journals Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly amongst IspD/IspE/IspF enzymes in the MEP pathway

2018 ◽  
Vol 38 (1) ◽  
Author(s):  
Zhongchuan Liu ◽  
Yun Jin ◽  
Weifeng Liu ◽  
Yong Tao ◽  
Ganggang Wang
Keyword(s):  
Bacillus Subtilis ◽  
Protein Complex ◽  
Isoprenoid Biosynthesis ◽  
Mep Pathway ◽  
Size Exclusion ◽  
Complex Assembly ◽  
Exclusion Chromatography ◽  
Key Enzyme ◽  
Accessible Surface ◽  
Protein Complex Assembly

2-C-Methyl-d-erythritol 2,4-cyclodiphosphate synthase (IspF) is a key enzyme in the 2-C-Methyl-d-erythritol-4-phosphate (MEP) pathway of isoprenoid biosynthesis. This enzyme catalyzes the 4-diphosphocytidyl-2-C-methyl-d-erythritol 2-phosphate (CDPME2P) to 2-C-methyl-d-erythritol 2,4-cyclodiphosphate (MEcDP) with concomitant release of cytidine 5′-diphospate (CMP). Bacillus subtilis is a potential host cell for the production of isoprenoids, but few studies are performed on the key enzymes of MEP pathway in B. subtilis. In this work, the high-resolution crystal structures of IspF in native and complex with CMP from B. subtilis have been determined. Structural comparisons indicate that there is a looser packing of the subunits of IspF in B. subtilis, whereas the solvent accessible surface of its active pockets is smaller than that in Escherichia coli. Meanwhile, the protein–protein associations of 2-C-Methyl-d-erythritol-4-phosphatecytidyltransferase (IspD), CDPME kinase (IspE) and IspF from B. subtilis and E. coli, which catalyze three consecutive steps in the MEP pathway, are analyzed by native gel shift and size exclusion chromatography methods. The data here show that protein complex assembly is not detectable. These results will be useful for isoprenoid biosynthesis by metabolic engineering.

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