scholarly journals scully, an Essential Gene of Drosophila, is Homologous to Mammalian Mitochondrial Type II l-3-hydroxyacyl-CoA Dehydrogenase/Amyloid-β Peptide-binding Protein

1998 ◽  
Vol 141 (4) ◽  
pp. 1009-1017 ◽  
Author(s):  
Laura Torroja ◽  
Daniel Ortuño-Sahagún ◽  
Alberto Ferrús ◽  
Barbara Hämmerle ◽  
Julio A. Barbas
Keyword(s):  
Germ Line ◽  
Essential Gene ◽  
Amyloid Β ◽  
Single Amino Acid ◽  
Amyloid Β Peptide ◽  
Type Ii ◽  
Phenotypic Analysis ◽  
Lipid Inclusions ◽  
Hydroxyacyl Coa Dehydrogenase

The characterization of scully, an essential gene of Drosophila with phenocritical phases at embryonic and pupal stages, shows its extensive homology with vertebrate type II l-3-hydroxyacyl-CoA dehydrogenase/ERAB. Genomic rescue demonstrates that four different lethal mutations are scu alleles, the molecular nature of which has been established. One of them, scu3127, generates a nonfunctional truncated product. scu4058 also produces a truncated protein, but it contains most of the known functional domains of the enzyme. The other two mutations, scu174 and scuS152, correspond to single amino acid changes. The expression of scully mRNA is general to many tissues including the CNS; however, it is highest in both embryonic gonadal primordia and mature ovaries and testes. Consistent with this pattern, the phenotypic analysis suggests a role for scully in germ line formation: mutant testis are reduced in size and devoid of maturing sperm, and mutant ovarioles are not able to produce viable eggs. Ultrastructural analysis of mutant spermatocytes reveals the presence of cytoplasmic lipid inclusions and scarce mitochondria. In addition, mutant photoreceptors contain morphologically aberrant mitochondria and large multilayered accumulations of membranous material. Some of these phenotypes are very similar to those present in human pathologies caused by β-oxidation disorders.

scholarly journals Single amino acid exchanges in separate domains of the Drosophila serendipity delta zinc finger protein cause embryonic and sex biased lethality.

Genetics ◽  
1992 ◽  
Vol 131 (4) ◽  
pp. 905-916 ◽  
Author(s):  
M Crozatier ◽  
K Kongsuwan ◽  
P Ferrer ◽  
J R Merriam ◽  
J A Lengyel ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Essential Gene ◽  
Larval Instar ◽  
Single Amino Acid ◽  
Isolation And Characterization ◽  
Finger Protein

Abstract The Drosophila serendipity (sry) delta (delta) zinc finger protein is a sequence-specific DNA binding protein, maternally inherited by the embryo and present in nuclei of transcriptionally active cells throughout fly development. We report here the isolation and characterization of four ethyl methanesulfate-induced zygotic lethal mutations of different strengths in the sry delta gene. For the stronger allele, all of the lethality occurs during late embryogenesis or the first larval instar. In the cases of the three weaker alleles, most of the lethality occurs during pupation; moreover, those adult escapers that emerge are sterile males lacking partially or completely in spermatozoa bundles. Genetic analysis of sry delta thus indicates that it is an essential gene, whose continued expression throughout the life cycle, notably during embryogenesis and pupal stage, is required for viability. Phenotypic analysis of sry delta hemizygote escaper males further suggests that sry delta may be involved in regulation of two different sets of genes: genes required for viability and genes involved in gonadal development. All four sry delta alleles are fully rescued by a wild-type copy of sry delta, but not by an additional copy of the sry beta gene, reinforcing the view that, although structurally related, these two genes exert distinct functions. Molecular characterization of the four sry delta mutations revealed that these mutations correspond to single amino acid replacements in the sry delta protein. Three of these replacements map to the same (third out of seven) zinc finger in the carboxy-terminal DNA binding domain; interestingly, none affects the zinc finger consensus residues. The fourth mutation is located in the NH2-proximal part of the protein, in a domain proposed to be involved in specific protein-protein interactions.

Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/Amyloid-β binding alcohol dehydrogenase (ABAD)

2000 ◽  
Vol 303 (2) ◽  
pp. 311-327 ◽  
Author(s):  
A.J Powell ◽  
J.A Read ◽  
M.J Banfield ◽  
F Gunn-Moore ◽  
S.D Yan ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Amyloid Β ◽  
Type Ii ◽  
Hydroxyacyl Coa Dehydrogenase

Quenched hydrogen/deuterium exchange NMR characterization of amyloid-β peptide aggregates formed in the presence of Cu2+or Zn2+

FEBS Journal ◽  
2009 ◽  
Vol 276 (15) ◽  
pp. 4051-4060 ◽  
Author(s):  
Anders Olofsson ◽  
Malin Lindhagen-Persson ◽  
Monika Vestling ◽  
A. Elisabeth Sauer-Eriksson ◽  
Anders Öhman
Keyword(s):  
Amyloid Β ◽  
Deuterium Exchange ◽  
Amyloid Β Peptide ◽  
Hydrogen Deuterium Exchange ◽  
Nmr Characterization ◽  
Hydrogen Deuterium

scholarly journals Characterization of the Binding of Amyloid-β Peptide to Cell Culture-Derived Native Apolipoprotein E2, E3, and E4 Isoforms and to Isoforms from Human Plasma

2002 ◽  
Vol 68 (2) ◽  
pp. 721-725 ◽  
Author(s):  
Dun-Sheng Yang ◽  
Jonathan D. Smith ◽  
Zhongmin Zhou ◽  
Samuel E. Gandy ◽  
Ralph N. Martins
Keyword(s):  
Cell Culture ◽  
Human Plasma ◽  
Amyloid Β ◽  
Amyloid Β Peptide

Identification and Nanomechanical Characterization of the HIV Tat‐Amyloid β Peptide Multifibrillar Structures

2020 ◽  
Vol 26 (43) ◽  
pp. 9449-9453
Author(s):  
Qiying Feng ◽  
Yue Hong ◽  
Naga Pradeep Nidamanuri ◽  
Chuanxu Yang ◽  
Qiang Li ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Hiv Tat

scholarly journals Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain L-3-hydroxyacyl-CoA dehydrogenase

1999 ◽  
Vol 345 (1) ◽  
pp. 139-143 ◽  
Author(s):  
Xue-Ying HE ◽  
Ying-Zi YANG ◽  
Horst SCHULZ ◽  
Song-Yu YANG
Keyword(s):  
Alcohol Dehydrogenase ◽  
Catalytic Properties ◽  
Amyloid Β ◽  
Hydroxysteroid Dehydrogenase ◽  
Amino Acid Sequences ◽  
Short Chain ◽  
Amyloid Β Peptide ◽  
Kinetic Measurements ◽  
Hydroxyacyl Coa Dehydrogenase ◽  
Adh Activity

The alcohol dehydrogenase (ADH) activity of human short-chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) has been characterized kinetically. The kcat of the purified enzyme was estimated to be 2.2 min-1, with apparent Km values of 280 mM and 22μM for 2-propanol and NAD+, respectively. The kcat of the ADH activity was three orders of magnitude less than the L-3-hydroxyacyl-CoA dehydrogenase activity but was comparable with that of the enzyme's hydroxysteroid dehydrogenase (HSD) activity for oxidizing 17β-oestradiol [He, Merz, Mehta, Schulz and Yang (1999) J. Biol. Chem. 274, 15014-15019]. However, the kcat values of intrinsic ADH and HSD activities of human SCHAD were found to be two orders of magnitude less than those reported for endoplasmic-reticulum-associated amyloid β-peptide-binding protein (ERAB) [Yan, Shi, Zhu, Fu, Zhu, Zhu, Gibson, Stern, Collison, Al-Mohanna et al. (1999) J. Biol. Chem. 274, 2145-2156]. Since human SCHAD and ERAB apparently possess identical amino acid sequences, their catalytic properties should be identical. The recombinant SCHAD has been confirmed to be the right gene product and not a mutant variant. Steady-state kinetic measurements and quantitative analyses reveal that assay conditions such as pH and concentrations of coenzyme and substrate do not account for the kinetic differences reported for ERAB and SCHAD. Rather problematic experimental procedures appear to be responsible for the unrealistically high catalytic rate constants of ERAB. Eliminating the confusion surrounding the catalytic properties of this important multifunctional enzyme paves the way for exploring its role(s) in the pathogenesis of Alzheimer's disease.

scholarly journals Characterization of stable complexes involving apolipoprotein E and the amyloid β peptide in Alzheimer's disease brain

Neuron ◽  
1995 ◽  
Vol 15 (1) ◽  
pp. 219-228 ◽  
Author(s):  
Jan Näslund ◽  
Johan Thyberg ◽  
Lars O. Tjernberg ◽  
Christer Wernstedt ◽  
Anders R. Karlström ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Apolipoprotein E ◽  
Amyloid Β ◽  
Amyloid Β Peptide
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