Skip header and navigation

Refine By

504 records – page 1 of 51.

The 3-hydroxyacyl-ACP dehydratase of mitochondrial fatty acid synthesis in Trypanosoma brucei.

https://arctichealth.org/en/permalink/ahliterature87070
Source
FEBS Lett. 2008 Mar 5;582(5):729-33
Publication Type
Article
Date
Mar-5-2008
Author
Autio Kaija J
Guler Jennifer L
Kastaniotis Alexander J
Englund Paul T
Hiltunen J Kalervo
Author Affiliation
Department of Biochemistry and Biocenter Oulu, University of Oulu, Oulu, Finland. kaija.autio@oulu.fi
Source
FEBS Lett. 2008 Mar 5;582(5):729-33
Date
Mar-5-2008
Language
English
Publication Type
Article
Keywords
Amino Acid Sequence
Animals
Electrophoresis
Fatty Acids - biosynthesis
Genetic Complementation Test
Humans
Hydro-Lyases - chemistry - isolation & purification - metabolism
Mitochondria - enzymology
Molecular Sequence Data
Protein Transport
Recombinant Fusion Proteins - isolation & purification - metabolism
Saccharomyces cerevisiae - cytology - metabolism
Sequence Alignment
Thioctic Acid - metabolism
Trypanosoma brucei brucei - cytology - enzymology
Abstract
The trypanosomatid parasite Trypanosoma brucei synthesizes fatty acids in the mitochondrion using the type II fatty acid synthesis (FAS) machinery. When mitochondrial FAS was characterized in T. brucei, all of the enzymatic components were identified based on their homology to yeast mitochondrial FAS enzymes, except for 3-hydroxyacyl-ACP dehydratase. Here we describe the characterization of T. brucei mitochondrial 3-hydroxyacyl-ACP dehydratase (TbHTD2), which was identified by its similarity to the human mitochondrial dehydratase. TbHTD2 can rescue the respiratory deficient phenotype of the yeast knock-out strain and restore the lipoic acid content, is localized in the mitochondrion and exhibits hydratase 2 activity.
PubMed ID
18258193 View in PubMed
Less detail

The 68K protease has beta-secretase-like activity for lymphocyte precursor protein but not for brain substrate.

https://arctichealth.org/en/permalink/ahliterature199515
Source
Neuroreport. 2000 Feb 7;11(2):373-7
Publication Type
Article
Date
Feb-7-2000
Author
A. Matsumoto
Author Affiliation
Department of Radiation Biophysics and Genetics, Kobe University School of Medicine, Japan.
Source
Neuroreport. 2000 Feb 7;11(2):373-7
Date
Feb-7-2000
Language
English
Publication Type
Article
Keywords
Aged
Aged, 80 and over
Alzheimer Disease - enzymology
Amino Acid Sequence
Amyloid Precursor Protein Secretases
Amyloid beta-Protein Precursor - metabolism
Aspartic Acid Endopeptidases - metabolism
Blotting, Western
Cells, Cultured
Cerebral Cortex - enzymology
Chondroitin ABC Lyase - metabolism
Endopeptidases
Female
Humans
Isoenzymes - metabolism
Lymphocytes - cytology - enzymology
Male
Middle Aged
Molecular Sequence Data
Organ Specificity
Peptide Fragments - chemistry
Polysaccharide-Lyases - metabolism
Protein Processing, Post-Translational
Sequence Analysis, Protein
Serine Endopeptidases - metabolism
Substrate Specificity
Abstract
Processing and metabolism of beta-amyloid precursor protein (APP) and generation of a variety of beta-amyloid (Abeta) peptides in the human brain is essentially associated with pathophysiology of Alzheimer's disease (AD). APP degradation activity of the 68 kDa serine protease, which was originally prepared from familial AD lymphoblastoid cells and harbors beta-secretase-like activity, was analyzed by Western blot using anti Abeta 1/40 antibody and anti APP cytoplasmic domain (CT) antibody. Native lymphocyte APP (LAPP) prepared from normal or AD-derived lymphoblastoid cells was degraded by the protease, generating a 16 kDa Abeta-bearing C-terminal fragment of APP. N-terminal amino acid sequencing of the fragment indicated that the protease cleaves LAPP at the Abeta-N-terminus. When the LAPP was treated with chondroitinase ABC prior to proteolysis, the activity to generate the fragment was inhibited, but pretreatment with heparitinase resulted in no effect. Native hippocampal APP prepared from normal brain, however, did not generate the 16 kDa peptide by the protease treatment. These results suggest that the process of APP degradation and Abeta-peptides generation, including beta-secretase activity, is associated with tissue specificity of both APP substrate and proteases. They also indicate that sulfated glycoconjugates attached to a portion of APP isoforms may play a role as a molecular determinant in the proteolysis.
PubMed ID
10674489 View in PubMed
Less detail

70 K type IV collagenase (gelatinase).

https://arctichealth.org/en/permalink/ahliterature24598
Source
Matrix Suppl. 1992;1:45-50
Publication Type
Article
Date
1992
Author
K. Tryggvason
P. Huhtala
M. Höyhtya
E. Hujanen
T. Hurskainen
Author Affiliation
Biocenter, University of Oulu, Finland.
Source
Matrix Suppl. 1992;1:45-50
Date
1992
Language
English
Publication Type
Article
Keywords
Amino Acid Sequence
Animals
Base Sequence
Basement Membrane - metabolism
Collagenases - chemistry - genetics - immunology - physiology
Gelatinase B
Genes
Humans
Molecular Sequence Data
Molecular Weight
Neoplasm Invasiveness
Neoplasm Proteins - physiology
Rabbits
Rats
Research Support, Non-U.S. Gov't
Sequence Alignment
Substrate Specificity
Abstract
Type IV collagenase (gelatinase) is a 70,000 dalton neutral metalloproteinase that specifically cleaves type IV collagen in addition to degrading denatured collagen (gelatin). It is secreted in a latent proenzyme form that is converted proteolytically in the extracellular space to a 62,000 dalton active enzyme. The primary structure, enzymatic properties as well as gene structure, demonstrate that type IV collagenase is closely related with the other well characterized metalloproteinases, interstitial collagenase and stromelysin. However, the structure of type IV collagenase differs from the others in that it is larger and contains three internal repeats that resemble the type II domains of fibronectin. Also, initial characterization of the promoter region of the gene indicates that its regulation differs from the other proteinase genes. Type IV collagenase is presumably required for the normal turnover of basement membranes. Augmented activity is linked with the invasive potential of tumor cells and the enzyme is believed to play a major role in the penetration of basement membranes by metastatic cells. Measurements of enzyme activity and mRNA levels as well as immunostaining of a variety of tumor cells and tissues suggest that assays for the enzyme may have value in the follow-up of malignant growth.
PubMed ID
1480085 View in PubMed
Less detail

Acceptable protective efficacy of influenza vaccination in young military conscripts under circumstances of incomplete antigenic and genetic match.

https://arctichealth.org/en/permalink/ahliterature194986
Source
Vaccine. 2001 Apr 30;19(23-24):3253-60
Publication Type
Article
Date
Apr-30-2001
Author
R. Pyhälä
M. Haanpää
M. Kleemola
R. Tervahauta
R. Visakorpi
L. Kinnunen
Author Affiliation
National Public Health Institute, Helsinki, Finland. reijo.pyhala@ktl.fi
Source
Vaccine. 2001 Apr 30;19(23-24):3253-60
Date
Apr-30-2001
Language
English
Publication Type
Article
Keywords
Adult
Amino Acid Sequence
Antibodies, Viral - blood
Antigens, Viral - genetics
Base Sequence
DNA Primers - genetics
Disease Outbreaks
Finland - epidemiology
Genes, Viral
Humans
Influenza A virus - genetics - immunology - isolation & purification
Influenza Vaccines - genetics - immunology - pharmacology
Influenza, Human - epidemiology - immunology - prevention & control - virology
Male
Military Personnel
Molecular Sequence Data
Phylogeny
Abstract
Commercial inactivated parenteral influenza vaccines reduced febrile (> or = 38 degrees C) respiratory illness by 53% (95% CL: 41-63%) during a 3 week outbreak in 1998 when A/Sydney/5/97(H3N2)-like influenza viruses were shown to be the predominant etiological agents and an older antigenic variant, A/Nanchang/933/95, served as the vaccine virus. The calculatory efficacy for preventing virologically diagnosed influenza infections was 57% (95% CL: 40-68%). The study population consisted of 1374 young male military conscripts. Vaccination coverage on a voluntary basis was 67%. Vaccination was ineffective in preventing febrile illness during a second epidemic wave lasting 2 weeks when mainly adenoviruses were shown to have been circulating in the garrison. Out of the 36 nasopharyngeal aspirates positive for influenza A by antigen detection, 18 A/Sydney/5/97-like strains (10 from non-vaccinated and eight from vaccinated subjects) and two A/Nanchang/933/95-like strains (both from non-vaccinated subjects) were isolated in MDCK cell cultures. Intraepidemic variation was detected among the A/Sydney/5/97-like field strains in their HA1 sequences and reactivity in HI tests, but no evidence was obtained that this variation would have been of significance to the virus in breaking through the vaccination-induced immunity.
PubMed ID
11312022 View in PubMed
Less detail

Additive effects of the mutations in the beta3-adrenergic receptor and uncoupling protein-1 genes on weight loss and weight maintenance in Finnish women.

https://arctichealth.org/en/permalink/ahliterature203645
Source
J Clin Endocrinol Metab. 1998 Dec;83(12):4246-50
Publication Type
Article
Date
Dec-1998
Author
M. Fogelholm
R. Valve
K. Kukkonen-Harjula
A. Nenonen
V. Hakkarainen
M. Laakso
M. Uusitupa
Author Affiliation
The UKK Institute for Health Promotion and Research, Tampere, Finland. mikael.fogelholm@helsinki.fi
Source
J Clin Endocrinol Metab. 1998 Dec;83(12):4246-50
Date
Dec-1998
Language
English
Publication Type
Article
Keywords
Adult
Amino Acid Sequence
Base Sequence
Body Weight - physiology
Carrier Proteins - genetics
Energy intake
Energy Metabolism - physiology
Female
Finland
Humans
Ion Channels
Membrane Proteins - genetics
Mitochondrial Proteins
Mutation - genetics - physiology
Receptors, Adrenergic, beta - genetics
Weight Loss - physiology
Abstract
This study examined whether the Trp64Arg mutation in the beta3-adrenergic receptor (beta3AR) and the A-->G mutation in the uncoupling protein-1 (UCP-1) genes have associations with weight loss and subsequent weight maintenance. Seventy-seven obese (body mass index range, 29-46 kg/m2), clinically healthy, premenopausal women were studied. A 12-wk weight reduction by very low calorie diet (VLCD) was followed by a 40-wk weight maintenance phase. The subjects were divided into four groups according to their beta3AR and UCP-1 genotype: no mutation (control; n=37), only Trp64Arg mutation in the beta3AR gene (n=12), only A-->G mutation in the UCP-1 gene (n=23), and both mutations (n=5). Subjects with both mutations had a lower weight reduction during VLCD than the controls [-10.5+/-0.6 (+/-SEM) vs. -14.0+/-0.5 kg; P=0.051, by ANOVA]. During the maintenance phase, weight in subjects with both mutations increased by 5.8+/-1.5 kg, but remained unchanged in the controls (-0.5+/-0.8 kg; P=0.041). The changes in weight in subjects with only one of the mutation were close to the results in the controls. Resting energy expenditure, adjusted for fat mass, fat-free mass, and maximal aerobic power, did not change differently between the groups throughout the study. The results suggest that a combination of the Trp64Arg mutation in the beta3AR and the A-->G mutation in the UCP-1 genes may be associated with faster weight gain after a VLCD.
PubMed ID
9851758 View in PubMed
Less detail

Adrenomyeloneuropathy: report of a new mutation in a French Canadian female.

https://arctichealth.org/en/permalink/ahliterature173849
Source
Can J Neurol Sci. 2005 May;32(2):261-3
Publication Type
Article
Date
May-2005
Author
Annie Dionne
Denis Brunet
Alexander McCampbell
Nicolas Dupré
Author Affiliation
Départment des Sciences Neurologiques, CHAUQ-Hôpital Enfant-Jésus, McGill University, QC, Canada.
Source
Can J Neurol Sci. 2005 May;32(2):261-3
Date
May-2005
Language
English
Publication Type
Article
Keywords
ATP-Binding Cassette Transporters - genetics
Adrenoleukodystrophy - genetics - metabolism - physiopathology
Amino Acid Sequence - genetics
Amino Acid Substitution - genetics
Chromosomes, Human, X - genetics
DNA Mutational Analysis
Diagnosis, Differential
Exons - genetics
Family Health
Female
Genetic Testing
Humans
Middle Aged
Mutation, Missense - genetics
Pedigree
Phenotype
Quebec - ethnology
Sex Factors
Abstract
X-linked adrenoleukodystrophy is a peroxisomial disorder caused by mutations in the ABCD1 gene. Adrenomyeloneuropathy is the second most frequent phenotype (25-46%) of this disease and classically presents in adulthood with spastic paraparesis. Female heterozygotes can be symptomatic, but they are frequently misdiagnosed as having multiple sclerosis.
We report a novel missense mutation in the ABCD1 gene in a 47-year-old French-Canadian female with spastic paraparesis and no confirmed family history of X-linked adrenoleukodystrophy. The mutation is located on exon 1 and causes the amino acid substitution of a valine for an alanine in a region of the protein highly conserved between mouse and man.
Adrenomyeloneuropathy must be considered in the differential diagnosis of spastic paraparesis in men or women. This is an initial report of an ABCD1 gene mutation in the French-Canadian population, which should lead to the recognition of other cases in the future.
PubMed ID
16018167 View in PubMed
Less detail

Aggregation and catabolism of disease-associated intra-Abeta mutations: reduced proteolysis of AbetaA21G by neprilysin.

https://arctichealth.org/en/permalink/ahliterature156321
Source
Neurobiol Dis. 2008 Sep;31(3):442-50
Publication Type
Article
Date
Sep-2008
Author
Vicki Betts
Malcolm A Leissring
Georgia Dolios
Rong Wang
Dennis J Selkoe
Dominic M Walsh
Author Affiliation
Laboratory for Neurodegenerative Research, The Conway Institute for Biomolecular and Biomedical Research, University College Dublin, Belfield, Dublin 4, Republic of Ireland.
Source
Neurobiol Dis. 2008 Sep;31(3):442-50
Date
Sep-2008
Language
English
Publication Type
Article
Keywords
Alzheimer Disease - genetics - metabolism - physiopathology
Amino Acid Sequence - genetics
Amino Acid Substitution - genetics
Amyloid beta-Peptides - chemistry - genetics - metabolism
Amyloid beta-Protein Precursor - chemistry - genetics - metabolism
Brain Chemistry - genetics
Fibrinolysin - chemistry - metabolism
Humans
Insulysin - chemistry - metabolism
Mass Spectrometry
Mutation - genetics
Neprilysin - chemistry - metabolism
Peptide Fragments - chemistry - genetics - metabolism
Peptide Hydrolases - metabolism
Plaque, Amyloid - chemistry - metabolism
Protein Structure, Tertiary - genetics
Abstract
Five point mutations within the amyloid beta-protein (Abeta) sequence of the APP gene are associated with hereditary diseases which are similar or identical to Alzheimer's disease and encode: the A21G (Flemish), E22G (Arctic), E22K (Italian), E22Q (Dutch) and the D23N (Iowa) amino acid substitutions. Although a substantial body of data exists on the effects of these mutations on Abeta production, whether or not intra-Abeta mutations alter degradation and how this relates to their aggregation state remain unclear. Here we report that the E22G, E22Q and the D23N substitutions significantly increase fibril nucleation and extension, whereas the E22K substitution exhibits only an increased rate of extension and the A21G substitution actually causes a decrease in the extension rate. These substantial differences in aggregation together with our observation that aggregated wild type Abeta(1-40) was much less well degraded than monomeric wild type Abeta(1-40), prompted us to assess whether or not disease-associated intra-Abeta mutations alter proteolysis independent of their effects on aggregation. Neprilysin (NEP), insulin degrading enzyme (IDE) and plasmin play a major role in Abeta catabolism, therefore we compared the ability of these enzymes to degrade wild type and mutant monomeric Abeta peptides. Experiments investigating proteolysis revealed that all monomeric peptides are degraded similarly by IDE and plasmin, but that the Flemish peptide was degraded significantly more slowly by NEP than wild type Abeta or any of the other mutant peptides. This finding suggests that resistance to NEP-mediated proteolysis may underlie the pathogenicity associated with the A21G mutation.
Notes
Cites: Nat Med. 2000 Feb;6(2):143-5010655101
Cites: J Neurochem. 2000 May;74(5):2209-1210800967
Cites: J Neurosci. 2000 Jun 1;20(11):3937-4610818128
Cites: Brain. 2000 Oct;123 ( Pt 10):2130-4011004129
Cites: Amyloid. 2000 Sep;7(3):166-7811019857
Cites: Nat Neurosci. 2001 Sep;4(9):887-9311528419
Cites: Neuron. 2001 Oct 25;32(2):177-8011683988
Cites: Nature. 2002 Apr 4;416(6880):535-911932745
Cites: J Neurochem. 2002 Apr;81(1):1-812067222
Cites: J Neurosci. 2003 Mar 15;23(6):1992-612657655
Cites: Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):4162-712634421
Cites: Proc Natl Acad Sci U S A. 2003 May 13;100(10):6221-612732730
Cites: Lancet. 2003 Jun 7;361(9373):1957-812801742
Cites: J Biol Chem. 2003 Jun 27;278(26):23221-612695513
Cites: Neurosci Lett. 2003 Oct 23;350(2):113-612972166
Cites: J Neurosci. 2003 Oct 1;23(26):8867-7114523088
Cites: Neuron. 2003 Dec 18;40(6):1087-9314687544
Cites: J Neurosci. 2004 Jan 28;24(4):991-814749444
Cites: Nat Neurosci. 2004 Sep;7(9):954-6015311281
Cites: Neurosci Lett. 2004 Sep 30;368(3):285-915364412
Cites: Neuron. 2004 Sep 30;44(1):181-9315450169
Cites: Neurosci Lett. 1993 Oct 14;161(1):17-207902973
Cites: J Neurol Neurosurg Psychiatry. 1995 Jun;58(6):699-7057608669
Cites: Peptides. 1995;16(4):647-527479298
Cites: Gene. 1995 Oct 27;164(2):363-67590358
Cites: J Neurochem. 1996 Feb;66(2):740-78592147
Cites: Anal Chem. 1996 Mar 1;68(5):850-88779443
Cites: Lab Invest. 1996 Feb;74(2):374-838780157
Cites: Biochem J. 2000 Jul 1;349(Pt 1):299-30810861242
Cites: Bioessays. 2001 Mar;23(3):261-911223883
Cites: Biochem J. 2001 May 1;355(Pt 3):869-7711311152
Cites: Science. 2001 May 25;292(5521):1550-211375493
Cites: J Biol Chem. 2001 Jun 15;276(24):21895-90111278416
Cites: Ann Neurol. 2001 Jun;49(6):697-70511409420
Cites: J Biol Chem. 2001 Aug 31;276(35):32860-611441013
Cites: Methods Enzymol. 1996;270:519-518803983
Cites: Neurochem Res. 1997 Jan;22(1):49-569021762
Cites: J Biol Chem. 1997 Aug 29;272(35):22364-729268388
Cites: FEBS Lett. 1998 May 8;427(2):153-69607302
Cites: J Biol Chem. 1998 Dec 4;273(49):32730-89830016
Cites: J Biol Chem. 1999 Sep 3;274(36):25945-5210464339
Cites: Nat Med. 2004 Nov;10(11):1190-215502844
Cites: Neurology. 2004 Nov 9;63(9):1613-715534244
Cites: Ann N Y Acad Sci. 2004 Dec;1035:1-2015681797
Cites: Trends Mol Med. 2005 Apr;11(4):170-615823755
Cites: Biochem Soc Trans. 2005 Nov;33(Pt 5):1101-516246055
Cites: Brain Res. 2007 Jun 4;1152:191-20017459354
Cites: Neurobiol Dis. 2007 Aug;27(2):164-7317566751
Cites: PLoS Med. 2007 Aug;4(8):e26217760499
Cites: Proc Natl Acad Sci U S A. 2007 Oct 16;104(42):16522-717940047
Cites: Peptides. 2007 Dec;28(12):2348-5517988763
PubMed ID
18602473 View in PubMed
Less detail

[Alpha 2-macroglobulin: structure, properties and physiological role]

https://arctichealth.org/en/permalink/ahliterature26949
Source
Ukr Biokhim Zh. 1983 Mar-Apr;55(2):218-33
Publication Type
Article
Author
K N Veremeenko
O S Semeniuta
A I Kizim
K A Lobunets
Source
Ukr Biokhim Zh. 1983 Mar-Apr;55(2):218-33
Language
Ukrainian
Publication Type
Article
Keywords
Amino Acid Sequence
Animals
Blood Protein Electrophoresis
Carbohydrates - analysis
Diagnosis, Differential
English Abstract
Hepatitis, Viral, Human - blood
Humans
Neoplasms - blood
Protease Inhibitors
Protein Conformation
Radiation Injuries, Experimental - drug therapy
Rats
Substrate Specificity
alpha-Macroglobulins - analysis - physiology - therapeutic use
Abstract
The paper is concerned with the results of recent researches devoted to studies of the structure, properties and physiological role of alpha 2-macroglobulin, one of main inhibitors of blood proteolytic enzymes. Data are presented on its primary and quaternary structure, mechanisms of interaction with proteinases. The role of alpha 2-macroglobulin in regulation of the activity of proteinases participating in blood coagulation, fibrinolysis, kininogenesis, immune reactions is shown. Possibilities of its application in medicine are discussed.
PubMed ID
6189273 View in PubMed
Less detail

Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis. Mutational and structural characterization of the active site and the fold.

https://arctichealth.org/en/permalink/ahliterature69307
Source
J Biol Chem. 2005 Apr 1;280(13):12611-20
Publication Type
Article
Date
Apr-1-2005
Author
Kalle Savolainen
Prasenjit Bhaumik
Werner Schmitz
Tiina J Kotti
Ernst Conzelmann
Rik K Wierenga
J Kalervo Hiltunen
Author Affiliation
Biocenter Oulu and Department of Biochemistry, University of Oulu, Linnanmaa, P. O. Box 3000, FIN-90014 University of Oulu, Finland.
Source
J Biol Chem. 2005 Apr 1;280(13):12611-20
Date
Apr-1-2005
Language
English
Publication Type
Article
Keywords
Alanine - chemistry
Amino Acid Sequence
Animals
Bile Acids and Salts - metabolism
Binding Sites
Catalysis
Circular Dichroism
Cloning, Molecular
Crystallography, X-Ray
Dimerization
Escherichia coli - metabolism
Models, Chemical
Models, Molecular
Molecular Sequence Data
Mutation
Mycobacterium tuberculosis - enzymology - genetics
Protein Conformation
Protein Folding
Protein Structure, Secondary
Racemases and Epimerases - chemistry - genetics
Rats
Research Support, Non-U.S. Gov't
Sequence Homology, Amino Acid
Substrate Specificity
Ultraviolet Rays
Abstract
Alpha-methylacyl-CoA racemase (Amacr) catalyzes the racemization of alpha-methyl-branched CoA esters. Sequence comparisons have shown that this enzyme is a member of the family III CoA transferases. The mammalian Amacr is involved in bile acid synthesis and branched-chain fatty acid degradation. In human, mutated variants of Amacr have been shown to be associated with disease states. Amino acid sequence alignment of Amacrs and its homologues from various species revealed 26 conserved protic residues, assumed to be potential candidates as catalytic residues. Amacr from Mycobacterium tuberculosis (MCR) was taken as a representative of the racemases. To determine their importance for efficient catalysis, each of these 26 protic residues of MCR was mutated into an alanine, respectively, and the mutated variants were overexpressed in Escherichia coli. It was found that four variants (R91A, H126A, D156A, and E241A) were properly folded but had much decreased catalytic efficiency. Apparently, Arg91, His126, Asp156, and Glu241 are important catalytic residues of MCR. The importance of these residues for catalysis can be rationalized by the 1.8 A resolution crystal structure of MCR, which shows that the catalytic site is at the interface between the large and small domain of two different subunits of the dimeric enzyme. This crystal structure is the first structure of a complete enzyme of the bile acid synthesis pathway. It shows that MCR has unique structural features, not seen in the structures of the sequence related formyl-CoA transferases, suggesting that the family III CoA transferases can be subdivided in at least two classes, being racemases and CoA transferases.
PubMed ID
15632186 View in PubMed
Less detail

Alterations in chlorophyll a/b binding proteins in Solanaceae cybrids.

https://arctichealth.org/en/permalink/ahliterature69077
Source
Mol Gen Genet. 1995 Dec 20;249(6):648-54
Publication Type
Article
Date
Dec-20-1995
Author
E. Babiychuk
R. Schantz
N. Cherep
J H Weil
Y. Gleba
S. Kushnir
Author Affiliation
Institute of Cell Biology and Genetic Engineering, Kiev, Ukraine.
Source
Mol Gen Genet. 1995 Dec 20;249(6):648-54
Date
Dec-20-1995
Language
English
Publication Type
Article
Keywords
Amino Acid Sequence
Carrier Proteins - chemistry - genetics - metabolism
Cell Compartmentation
Cell Nucleus - genetics
Chimera
Chloroplasts - genetics
Gene Expression
Genes, Plant
Hybrid Cells
Light-Harvesting Protein Complexes
Molecular Sequence Data
Multigene Family
Photosynthetic Reaction Center Complex Proteins - chemistry - genetics - metabolism
Photosystem II Protein Complex
Plant Proteins
Plants - genetics
Plants, Toxic
Research Support, Non-U.S. Gov't
Sequence Analysis
Sequence Homology, Amino Acid
Tobacco - genetics
Variation (Genetics)
Abstract
In this study we have constructed a number of plants (cybrids), in which the nuclear genome of Nicotiana plumbaginifolia is combined with the plastome of Atropa belladonna, or the nuclear genome of N. tabacum with plastomes of Lycium barbarum, Scopolia carniolica, Physochlaine officinalis or Nolana paradoxa. Our biochemical and immunological analyses prove that in these cybrids the biogenesis of the chlorophyll a/b binding proteins (CAB) of the light harvesting complex II (LHCII) is altered. Besides normal sized CAB polypeptides of 27, 25.5 and 25 kDa, which become less abundant, the cybrids analyzed have additional polypeptides of 26, 24.5 and 24 kDa. Direct protein micro-sequencing showed that at least two truncated 26 kDa CAB polypeptides in plant cells containing a nucleus of N. plumbaginifolia and plastids of A. belladonna are encoded by the type 1 Lhcb genes. These polypeptides are 11-12 amino acids shorter at the N-terminus than the expected size. Based on the available data we conclude that the biogenesis of the LHCII in vivo may depend on plastome-encoded factor(s). These results suggest that plastome-encoded factors that cause specific protein degradation and/or abnormal processing might determine compartmental genetic incompatibility in plants.
PubMed ID
8544830 View in PubMed
Less detail

504 records – page 1 of 51.