Mutational Analysis of the Four α-Helix Bundle Iron-Loading Channel of Rat Liver Ferritin

1998 ◽  
Vol 352 (1) ◽  
pp. 71-77 ◽  
Author(s):  
Jia-Hsin Guo ◽  
Shu-Hui Juan ◽  
Steven D. Aust
Keyword(s):  
Rat Liver ◽  
Mutational Analysis ◽  
Iron Loading ◽  
Helix Bundle ◽  
Α Helix ◽  
Liver Ferritin

scholarly journals The helix bundle domain of primase RepB’ is required for dinucleotide formation and extension

2020 ◽  
Author(s):  
Sofia Banchenko ◽  
Chris Weise ◽  
Erich Lanka ◽  
Wolfram Saenger ◽  
Sebastian Geibel
Keyword(s):  
Dna Replication ◽  
Transfer Reaction ◽  
Catalytic Domain ◽  
Mutational Analysis ◽  
Dna Polymerases ◽  
Critical Role ◽  
Helix Bundle ◽  
Dna Strand ◽  
Α Helix ◽  
Template Dna

ABSTRACTDuring DNA replication, primases synthesize oligonucleotide primers on single-stranded template DNA, which are then extended by DNA polymerases to synthesize a complementary DNA strand. Primase RepB’ of plasmid RSF1010 initiates DNA replication on two 40 nucleotide long inverted repeats, termed ssiA and ssiB, within the oriV of RSF1010. RepB’ consists of a catalytic domain and a helix bundle domain which are connected by long α-helix 6 and an unstructured linker. Previous work has demonstrated that RepB’ requires both domains for initiation of dsDNA synthesis in DNA replication assays. However, the precise functions of these two domains in primer synthesis have been unknown. Here we report that both domains of RepB’ are required to synthesizes a 10–12 nucleotide long DNA primer whereas the isolated domains are inactive. Mutational analysis of the catalytic domain indicates that the solvent-exposed W50 plays a critical role in resolving a hairpin structures formed by ssiA and ssiB. Three structurally conserved aspartates (D77, D78 and D134) of RepB’ catalyse the nucleotidyl transfer reaction. Mutations on the helix bundle domain are identified that either reduce the primer length to a dinucleotide (R285A) or abolish primer synthesis (D238A) indicating that the helix bundle domain is required to form and extend the initial dinucleotide synthesized by the catalytic domain.

Comparison of cytosolic products formed in rat liver in response to parenteral and dietary iron loading

1992 ◽  
Vol 35 (1) ◽  
pp. 47-54 ◽  
Author(s):  
P. L. Ringeling ◽  
M. I. Cleton ◽  
M. I. E. Huijskes-Heins ◽  
W. C. de Bruijn ◽  
H. G. van Eijk
Keyword(s):  
Rat Liver ◽  
Dietary Iron ◽  
Iron Loading

De NovoDesign and Synthesis of Four α-Helix Bundle Proteins with Flavin Function

1993 ◽  
Vol 22 (9) ◽  
pp. 1533-1536 ◽  
Author(s):  
Hisakazu Mihara ◽  
Kin-ya Tomizaki ◽  
Norikazu Nishino ◽  
Tsutomu Fujimoto
Keyword(s):  
Helix Bundle ◽  
Α Helix

scholarly journals Protein Evolution across Fold Classes: A 3-α-Helix Bundle can Switch to β, α/β, and α+β Folds by Stepwise Mutation

2015 ◽  
Vol 108 (2) ◽  
pp. 203a-204a
Author(s):  
Lauren L. Porter ◽  
Yanan He ◽  
Yihong Chen ◽  
John Orban ◽  
Philip N. Bryan
Keyword(s):  
Protein Evolution ◽  
Helix Bundle ◽  
Stepwise Mutation ◽  
Α Helix

The Isoferritin Composition of Rat Liver During Bleeding Induced Catabolism of Liver Ferritin

1984 ◽  
pp. 199-202
Author(s):  
F.M.J. ZUYDERHOUDT ◽  
P.L.M. VIJVERBERG ◽  
W.O. SCHREUDER ◽  
C. LINTHORST ◽  
G.G.A. JÖRNING
Keyword(s):  
Rat Liver ◽  
Liver Ferritin
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