scholarly journals Biochemical analysis of the interactions of IQGAP1 C-terminal domain with CDC42

2012 ◽  
Vol 3 (3) ◽  
pp. 53 ◽  
Author(s):  
Sarah F Elliott
Keyword(s):  
Biochemical Analysis ◽  
Terminal Domain

scholarly journals Biochemical analysis of the N-terminal domain of human RAD54B

2008 ◽  
Vol 36 (17) ◽  
pp. 5441-5450 ◽  
Author(s):  
N. Sarai ◽  
W. Kagawa ◽  
N. Fujikawa ◽  
K. Saito ◽  
J. Hikiba ◽  
...  
Keyword(s):  
Biochemical Analysis ◽  
Terminal Domain

scholarly journals Biochemical analysis of human PIF1 helicase and functions of its N-terminal domain

2008 ◽  
Vol 36 (19) ◽  
pp. 6295-6308 ◽  
Author(s):  
Yongqing Gu ◽  
Yuji Masuda ◽  
Kenji Kamiya
Keyword(s):  
Biochemical Analysis ◽  
Terminal Domain ◽  
Pif1 Helicase

scholarly journals Insights into EB1 structure and the role of its C-terminal domain for discriminating microtubule tips from the lattice

2011 ◽  
Vol 22 (16) ◽  
pp. 2912-2923 ◽  
Author(s):  
Rubén M. Buey ◽  
Renu Mohan ◽  
Kris Leslie ◽  
Thomas Walzthoeni ◽  
John H. Missimer ◽  
...  
Keyword(s):  
Biochemical Analysis ◽  
Binding Proteins ◽  
Coiled Coil ◽  
Actin Binding ◽  
Terminal Domain ◽  
X Ray Scattering ◽  
C Terminus ◽  
Stable Association ◽  
Chemical Cross Linking

End-binding proteins (EBs) comprise a conserved family of microtubule plus end–tracking proteins. The concerted action of calponin homology (CH), linker, and C-terminal domains of EBs is important for their autonomous microtubule tip tracking, regulation of microtubule dynamics, and recruitment of numerous partners to microtubule ends. Here we report the detailed structural and biochemical analysis of mammalian EBs. Small-angle X-ray scattering, electron microscopy, and chemical cross-linking in combination with mass spectrometry indicate that EBs are elongated molecules with two interacting CH domains, an arrangement reminiscent of that seen in other microtubule- and actin-binding proteins. Removal of the negatively charged C-terminal tail did not affect the overall conformation of EBs; however, it increased the dwell times of EBs on the microtubule lattice in microtubule tip–tracking reconstitution experiments. An even more stable association with the microtubule lattice was observed when the entire negatively charged C-terminal domain of EBs was replaced by a neutral coiled-coil motif. In contrast, the interaction of EBs with growing microtubule tips was not significantly affected by these C-terminal domain mutations. Our data indicate that long-range electrostatic repulsive interactions between the C-terminus and the microtubule lattice drive the specificity of EBs for growing microtubule ends.

scholarly journals Biochemical and functional characterization of a meiosis-specific Pch2/ORC AAA+ assembly

2020 ◽  
Vol 3 (11) ◽  
pp. e201900630
Author(s):  
María Ascensión Villar-Fernández ◽  
Richard Cardoso da Silva ◽  
Magdalena Firlej ◽  
Dongqing Pan ◽  
Elisabeth Weir ◽  
...  
Keyword(s):  
Biochemical Analysis ◽  
Budding Yeast ◽  
Functional Characterization ◽  
Efficient Removal ◽  
Terminal Domain ◽  
Origins Of Replication ◽  
Mcm Helicase ◽  
A Subunit ◽  
Aaa Protein

Pch2 is a meiosis-specific AAA+ protein that controls several important chromosomal processes. We previously demonstrated that Orc1, a subunit of the ORC, functionally interacts with budding yeast Pch2. The ORC (Orc1-6) AAA+ complex loads the AAA+ MCM helicase to origins of replication, but whether and how ORC collaborates with Pch2 remains unclear. Here, we show that a Pch2 hexamer directly associates with ORC during the meiotic G2/prophase. Biochemical analysis suggests that Pch2 uses its non-enzymatic NH2-terminal domain and AAA+ core and likely engages the interface of ORC that also binds to Cdc6, a factor crucial for ORC-MCM binding. Canonical ORC function requires association with origins, but we show here that despite causing efficient removal of Orc1 from origins, nuclear depletion of Orc2 and Orc5 does not trigger Pch2/Orc1-like meiotic phenotypes. This suggests that the function for Orc1/Pch2 in meiosis can be executed without efficient association of ORC with origins of replication. In conclusion, we uncover distinct functionalities for Orc1/ORC that drive the establishment of a non-canonical, meiosis-specific AAA+ assembly with Pch2.

scholarly journals Functional and Biochemical Analysis of the N-terminal Domain of Phytochrome A

2006 ◽  
Vol 281 (45) ◽  
pp. 34421-34429 ◽  
Author(s):  
Julieta L. Mateos ◽  
Juan Pablo Luppi ◽  
Ouliana B. Ogorodnikova ◽  
Vitaly A. Sineshchekov ◽  
Marcelo J. Yanovsky ◽  
...  
Keyword(s):  
Biochemical Analysis ◽  
Phytochrome A ◽  
Terminal Domain

scholarly journals A meiosis-specific AAA+ assembly reveals repurposing of ORC during budding yeast gametogenesis

2019 ◽  
Author(s):  
María Ascensión Villar-Fernández ◽  
Richard Cardoso da Silva ◽  
Dongqing Pan ◽  
Elisabeth Weir ◽  
Annika Sarembe ◽  
...  
Keyword(s):  
Biochemical Analysis ◽  
Budding Yeast ◽  
Replication Origins ◽  
Terminal Domain ◽  
Binding Interface ◽  
Mcm Helicase ◽  
A Subunit ◽  
Per Se ◽  
Aaa Protein

ABSTRACTORC (Orc1-6) is an AAA+ complex that loads the AAA+ MCM helicase to replication origins. Orc1, a subunit of ORC, functionally interacts with budding yeast Pch2, a meiosis-specific AAA+ protein. Pch2 regulates several chromosomal events of gametogenesis, but mechanisms that dictate Pch2 function remain poorly understood. We demonstrate that ORC directly interacts with an AAA+ Pch2 hexamer. The ORC-Pch2 assembly is established without Cdc6, a factor crucial for ORC-MCM binding. Biochemical analysis suggests that Pch2 utilizes ORC’s Cdc6-binding interface and employs its non-enzymatic NH2-terminal domain and AAA+ core to engage ORC. In contrast to phenotypes observed upon Orc1 impairment, nuclear depletion of other subunits of ORC does not lead to Pch2-like phenotypes, indicating that ORC integrity per se is not required to support Pch2 function. We thus reveal functional interplay between Pch2 and ORC, and uncover the repurposing of ORC to establish a non-canonical and meiosis-specific AAA+ assembly.

scholarly journals Genetic and biochemical analysis of the adenylyl cyclase-associated protein, cap, in Schizosaccharomyces pombe.

1992 ◽  
Vol 3 (2) ◽  
pp. 167-180 ◽  
Author(s):  
M Kawamukai ◽  
J Gerst ◽  
J Field ◽  
M Riggs ◽  
L Rodgers ◽  
...  
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Adenylyl Cyclase ◽  
Biochemical Analysis ◽  
Slow Growth ◽  
Proper Function ◽  
Adenylyl Cyclase Activity ◽  
Yeast Saccharomyces Cerevisiae ◽  
Terminal Domain ◽  
Cellular Responsiveness ◽  
Entire Gene

We have identified, cloned, and studied a gene, cap, encoding a protein that is associated with adenylyl cyclase in the fission yeast Schizosaccharomyces pombe. This protein shares significant sequence homology with the adenylyl cyclase-associated CAP protein in the yeast Saccharomyces cerevisiae. CAP is a bifunctional protein; the N-terminal domain appears to be involved in cellular responsiveness to RAS, whereas loss of the C-terminal portion is associated with morphological and nutritional defects. S. pombe cap can suppress phenotypes associated with deletion of the C-terminal CAP domain in S. cerevisiae but does not suppress phenotypes associated with deletion of the N-terminal domain. Analysis of cap disruptants also mapped the function of cap to two domains. The functional loss of the C-terminal region of S. pombe cap results in abnormal cellular morphology, slow growth, and failure to grow at 37 degrees C. Increases in mating and sporulation were observed when the entire gene was disrupted. Overproduction of both cap and adenylyl cyclase results in highly elongated large cells that are sterile and have measurably higher levels of adenylyl cyclase activity. Our results indicate that cap is required for the proper function of S. pombe adenylyl cyclase but that the C-terminal domain of cap has other functions that are shared with the C-terminal domain of S. cerevisiae CAP.

Mitochondria in Cardiomyopathy: Alterations in Size, Number and Internal Structures

1968 ◽  
Vol 26 ◽  
pp. 126-127
Author(s):  
George Hug ◽  
William K. Schubert
Keyword(s):  
Heart Failure ◽  
Biochemical Analysis ◽  
Left Ventricular ◽  
Size Number ◽  
Internal Structures ◽  
Left Ventricular Outflow ◽  
Chest X Ray ◽  
Myocardial Fibers ◽  
Muscle Biopsies ◽  
Needle Liver Biopsy

A white boy six months of age was hospitalized with respiratory distress and congestive heart failure. Control of the heart failure was achieved but marked cardiomegaly, moderate hepatomegaly, and minimal muscular weakness persisted.At birth a chest x-ray had been taken because of rapid breathing and jaundice and showed the heart to be of normal size. Clinical studies included: EKG which showed biventricular hypertrophy, needle liver biopsy which showed toxic hepatitis, and cardiac catheterization which showed no obstruction to left ventricular outflow. Liver and muscle biopsies revealed no biochemical or histological evidence of type II glycogexiosis (Pompe's disease). At thoracotomy, 14 milligrams of left ventricular muscle were removed. Total phosphorylase activity in the biopsy specimen was normal by biochemical analysis as was the degree of phosphorylase activation. By light microscopy, vacuoles and fine granules were seen in practically all myocardial fibers. The fibers were not hypertrophic. The endocardium was not thickened excluding endocardial fibroelastosis. Based on these findings, the diagnosis of idiopathic non-obstructive cardiomyopathy was made.

3H-galactose and 3H-glucose incorporation into newly synthesized hepatic glycogen in control-fed rats

1986 ◽  
Vol 44 ◽  
pp. 292-293
Author(s):  
J.E. Michaels ◽  
S.A. Garfield ◽  
J.T. Hung ◽  
S.S. Smith ◽  
R.R. Cardell
Keyword(s):  
Biochemical Analysis ◽  
Glycogen Synthesis ◽  
Hepatic Glycogen ◽  
Electron Microscopic ◽  
Once Daily ◽  
Tail Vein ◽  
Tracer Dose ◽  
Glucose Incorporation ◽  
Wet Weight

3H-galactose (gal) and 3H-glucose (glu) were compared to determine which compound was preferable for pulse labeling newly formed hepatic glycogen. Control fed rats were used to achieve substantial and consistent levels of hepatic glycogen and to stimulate glycogen synthesis.Rats fed once daily for 4 hr achieved hepatic glycogen levels > 3% wet weight liver prior to injection by tail vein of a tracer dose of 3H-gal or 3H-glu. The rats were sacrificed 15-120 min later and liver was prepared by routine techniques for light (LM) and electron microscopic (EM) radioautography (RAG) and biochemical analysis.

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