Deletion Mutagenesis and Identification of Causative Mutations in Maize

2017 ◽  
pp. 97-108 ◽  
Author(s):  
Shangang Jia ◽  
Aixia Li ◽  
Chi Zhang ◽  
David Holding
Keyword(s):  
Deletion Mutagenesis

Deletion mutagenesis of rat PC12 tyrosine hydroxylase regulatory and catalytic domains

1993 ◽  
Vol 4 (2) ◽  
pp. 125-139 ◽  
Author(s):  
Paula Ribeiro ◽  
Yuehua Wang ◽  
Bruce A. Citron ◽  
Seymour Kaufman
Keyword(s):  
Tyrosine Hydroxylase ◽  
Deletion Mutagenesis ◽  
Catalytic Domains

Site-directed deletion mutagenesis within the T4 endonuclease V gene: dispensable sequences within putative loop regions

1991 ◽  
Vol 255 (1) ◽  
pp. 19-29 ◽  
Author(s):  
M.L. Dodson ◽  
Melissa A. Prince ◽  
Wayne F. Anderson ◽  
R.Stephen Lloyd
Keyword(s):  
Deletion Mutagenesis ◽  
Endonuclease V ◽  
Loop Regions ◽  
V Gene

Deletion mutagenesis in M13 by polymerase chain reaction using universal sequencing primers

1990 ◽  
Vol 188 (2) ◽  
pp. 255-258 ◽  
Author(s):  
E. Tannich ◽  
M. Tümmler ◽  
H.H. Arnold ◽  
K. Lingelbach
Keyword(s):  
Polymerase Chain Reaction ◽  
Chain Reaction ◽  
Deletion Mutagenesis ◽  
Polymerase Chain

scholarly journals Are the conserved sequences in segment 1 of gelsolin important for binding actin?

1992 ◽  
Vol 116 (5) ◽  
pp. 1135-1143 ◽  
Author(s):  
M Way ◽  
B Pope ◽  
A G Weeds
Keyword(s):  
Direct Interaction ◽  
Actin Binding ◽  
Amino Acid Substitutions ◽  
Interaction Site ◽  
Conserved Sequences ◽  
Functional Sites ◽  
Deletion Mutagenesis ◽  
Polar Groups ◽  
Charged Residues ◽  
Minimal Region

The minimal region required for actin binding in the smallest of the three domains of gelsolin (termed Segment 1 or S1) was previously defined by deletion mutagenesis as residues 37-126. Further analysis of NH2-terminal deletions here redefines the minimal functional core as residues 41-126. Amino acid substitutions within this core further elucidate the nature of the interaction of segment 1 with actin. Of 26 point mutants analyzed, 14 reduced the affinity for actin. The charged residues His 119, Arg 120, Glu 121, and Gln 123 appear to be involved in direct interaction with actin. Substitutions of Leu 108, Leu 112, and Val 117 by polar groups all affect the structural stability of segment 1 and thereby reduce binding affinity. In addition replacement of Glu 126 by aspartic acid modifies the physical properties of segment 1 and weakens binding. We have further shown that changing charged residues within the highly conserved pentapeptide sequence LDDYL (residues 108-112) has no effect on actin binding. This sequence, found in a number of different actin binding proteins, does not therefore constitute part of the interaction site. Similarly, substitution of the two acidic residues by basic ones within the DESG motif of segment 1 (residues 96-99, but also found near the COOH terminus of actin) does not impair binding. These results show the dangers of predicting functional sites on the basis of conserved sequences.

scholarly journals Characterization of a yeast mitochondrial promoter by deletion mutagenesis.

1985 ◽  
Vol 82 (7) ◽  
pp. 1954-1958 ◽  
Author(s):  
T. K. Biswas ◽  
J. C. Edwards ◽  
M. Rabinowitz ◽  
G. S. Getz
Keyword(s):  
Deletion Mutagenesis

Random Insertion and Deletion Mutagenesis

2003 ◽  
pp. 53-64 ◽  
Author(s):  
Hiroshi Murakami ◽  
Takahiro Hohsaka ◽  
Masahiko Sisido
Keyword(s):  
Deletion Mutagenesis ◽  
Insertion And Deletion ◽  
Random Insertion

scholarly journals Prominent Binding of Human and Equine Fibrinogen to Streptococcus equi subsp. zooepidemicus Is Mediated by Specific SzM Types and Is a Distinct Phenotype of Zoonotic Isolates

2019 ◽  
Vol 88 (1) ◽  
Author(s):  
René Bergmann ◽  
Maria-Christin Jentsch ◽  
Albrecht Uhlig ◽  
Uwe Müller ◽  
Mark van der Linden ◽  
...  
Keyword(s):  
Plasma Proteins ◽  
Human Origins ◽  
Flow Cytometry Analysis ◽  
Human Fibrinogen ◽  
Content Type ◽  
Bacterial Surface ◽  
Distinct Phenotype ◽  
Deletion Mutagenesis ◽  
Streptococcus Equi ◽  
High Degree

ABSTRACTStreptococcus equi subsp. zooepidemicus is an important pathogen in horses that causes severe diseases such as pneumonia and abortion. Furthermore, it is a zoonotic agent, and contact with horses is a known risk factor. In this study, we investigated the working hypothesis that the zoonotic potential varies among S. equi subsp. zooepidemicus strains in association with differences in M-like protein-mediated binding of host plasma proteins. We demonstrate via in-frame deletion mutagenesis of two different S. equi subsp. zooepidemicus strains that the M-like protein SzM is crucial for the binding of fibrinogen to the bacterial surface and for survival in equine and human blood. S. equi subsp. zooepidemicus isolates of equine and human origins were compared with regard to SzM sequences and binding of equine and human fibrinogens. The N-terminal 216 amino acids of the mature SzM were found to exhibit a high degree of diversity, but the majority of human isolates grouped in three distinct SzM clusters. Plasma protein absorption assays and flow cytometry analysis revealed that pronounced binding of human fibrinogen is a common phenotype of human S. equi subsp. zooepidemicus isolates but much less so in equine S. equi subsp. zooepidemicus isolates. Furthermore, binding of human fibrinogen is associated with specific SzM types. These results suggest that SzM-mediated binding of human fibrinogen is an important virulence mechanism of zoonotic S. equi subsp. zooepidemicus isolates.

scholarly journals Specific Sites in the Cytoplasmic N Terminus Modulate Conformational Transitions of the Na,K-ATPase

2007 ◽  
Vol 282 (46) ◽  
pp. 33691-33697 ◽  
Author(s):  
Rosemarie Scanzano ◽  
Laura Segall ◽  
Rhoda Blostein
Keyword(s):  
Steady State ◽  
Conformational Equilibrium ◽  
Conformational Transitions ◽  
Catalytic Cycle ◽  
Flexible Structure ◽  
Atp Binding ◽  
Deletion Mutagenesis ◽  
N Terminus

The cytoplasmic N terminus of the Na,K-ATPase is a highly charged and flexible structure that comprises three predicted helical regions including H1 spanning residues 27 to 33 and H2 spanning residues 42 to 50. Previous deletion mutagenesis experiments showed that deletion of residues up to and including most of H2 shifts the E1/E2 conformational equilibrium toward E1. The present study describes a clustered charge-to-alanine mutagenesis approach designed to delineate specific sites within the N terminus that modulate the steady-state E1 ↔ E2 and E1P ↔ E2P poise. Criteria to assess shifts in poise include (i) sensitivity to inhibition by inorganic orthovanadate to assess overall poise; (ii) K+-sensitivity of Na-ATPase measured at micromolar ATP to assess changes in the E2(K) + ATP → E1·ATP + K+ rate; (iii) K′ATP for low-affinity ATP binding at the latter step; (iv) overall catalytic turnover, and (v) the E1P → E2P transition. The results of alanine replacements in H1 (31KKE) suggest that this site stabilizes E2P and to a lesser extent E2. In H2, residues within 47HRK have a role in stabilizing E2 but not E2P as revealed with double mutants 31KKE → AAA/47H → A and 31KKE → AAA/47HRK → AAA. Taken together, these observations suggest that sites 31KKE in H1 and 47HRK in H2 have distinct roles in modulating the enzyme's conformational transitions during the catalytic cycle of the enzyme.

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