Cloning of a Genomic DNA Encoding Caffeoyl-coenzyme A 3-O-methyltransferase of Citrus

2000 ◽  
Vol 66 (2) ◽  
pp. 144-148 ◽  
Author(s):  
Alfredo Gryciuk ALMEIDA ◽  
Shinji TSUYUMU
Keyword(s):  
Genomic Dna ◽  
Coenzyme A ◽  
Dna Encoding

scholarly journals Biochemical Analysis of Lpt3, a Protein Responsible forPhosphoethanolamine Addition to Lipooligosaccharide ofPathogenic Neisseria

2006 ◽  
Vol 188 (3) ◽  
pp. 1039-1048 ◽  
Author(s):  
Ellen T. O'Connor ◽  
Andrzej Piekarowicz ◽  
Karen V. Swanson ◽  
J. McLeod Griffiss ◽  
Daniel C. Stein
Keyword(s):  
Genomic Dna ◽  
Biochemical Analysis ◽  
Expression Vector ◽  
Inner Core ◽  
Genomic Sequence ◽  
Mass Spectrometry Analysis ◽  
Dna Encoding ◽  
Spectrometry Analysis ◽  
Transposon Insertion ◽  
Genomic Dna Sequence

ABSTRACT The inner core of neisserial lipooligosaccharide (LOS) contains heptose residues that can be decorated by phosphoethanolamine (PEA). PEA modification of heptose II (HepII) can occur at the 3, 6, or 7 position(s). We used a genomic DNA sequence of lpt3, derived from Neisseria meningitidis MC58, to search the genomic sequence of N. gonorrhoeae FA1090 and identified a homolog of lpt3 in N. gonorrhoeae. A PCR amplicon containing lpt3 was amplified from F62ΔLgtA, cloned, mutagenized, and inserted into the chromosome of N. gonorrhoeae strain F62ΔLgtA, producing strain F62ΔLgtAlpt3::Tn5. LOS isolated from this strain lost the ability to bind monoclonal antibody (MAb) 2-1-L8. Complementation of this mutation by genetic removal of the transposon insertion restored MAb 2-1-L8 binding. Mass spectrometry analysis of LOS isolated from the F62ΔLgtA indicated that this strain contained two PEA modifications on its LOS. F62ΔLgtAlpt3::Tn5 lacked a PEA modification on its LOS, a finding consistent with the hypothesis that lpt3 encodes a protein mediating PEA addition onto gonococcal LOS. The DNA encoding lpt3 was cloned into an expression vector and Lpt3 was purified. Purified Lpt3 was able to mediate the addition of PEA to LOS isolated from F62ΔLgtAlpt3::Tn5.

scholarly journals Molecular cloning and sequencing of genomic DNA encoding yeast vacuolar carboxypeptidase yscS

FEBS Letters ◽  
1991 ◽  
Vol 283 (1) ◽  
pp. 27-32 ◽  
Author(s):  
Javier Bordallo ◽  
Carmen Bordallo ◽  
Gascón Santiago ◽  
Paz Suárez-Rendueles
Keyword(s):  
Molecular Cloning ◽  
Genomic Dna ◽  
Dna Encoding ◽  
Cloning And Sequencing

Cloning and sequence analysis of calf cDNA and human genomic DNA encoding α-subunit precursor of muscle acetylcholine receptor

Nature ◽  
1983 ◽  
Vol 305 (5937) ◽  
pp. 818-823 ◽  
Author(s):  
Masaharu Noda ◽  
Yasuji Furutani ◽  
Hideo Takahashi ◽  
Mitsuyoshi Toyosato ◽  
Tsutomu Tanabe ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Acetylcholine Receptor ◽  
Genomic Dna ◽  
Dna Encoding ◽  
Α Subunit ◽  
Human Genomic ◽  
Human Genomic Dna

scholarly journals Molecular Cloning of a Genomic DNA Encoding Yam Class IV Chitinase

2004 ◽  
Vol 68 (7) ◽  
pp. 1508-1517 ◽  
Author(s):  
Takuji MITSUNAGA ◽  
Minoru IWASE ◽  
Wimal UBHAYASEKERA ◽  
Sherry L. MOWBRAY ◽  
Daizo KOGA
Keyword(s):  
Molecular Cloning ◽  
Genomic Dna ◽  
Dna Encoding ◽  
Class Iv Chitinase ◽  
Class Iv

scholarly journals Nucleotide Sequence for the Genomic DNA Encoding an Anionic Peroxidase Gene from a Hybrid Poplar,Populus kitakamiensis

1993 ◽  
Vol 57 (1) ◽  
pp. 131-133 ◽  
Author(s):  
Shinya Kawai ◽  
Yasuo Matsumoto ◽  
Shinya Kajita ◽  
Keiko Yamada ◽  
Yoshihiro Katayama ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Genomic Dna ◽  
Hybrid Poplar ◽  
Dna Encoding ◽  
Anionic Peroxidase ◽  
Peroxidase Gene

Insect immunity: molecular cloning, expression, and characterization of cDNAs and genomic DNA encoding three isoforms of insect defensin in Aedes aegypti

1999 ◽  
Vol 8 (1) ◽  
pp. 107-118 ◽  
Author(s):  
C. A. Lowenberger ◽  
C. T. Smartt ◽  
P. Bulet ◽  
M. T. Ferdig ◽  
D. W. Severson ◽  
...  
Keyword(s):  
Aedes Aegypti ◽  
Molecular Cloning ◽  
Genomic Dna ◽  
Insect Immunity ◽  
Dna Encoding ◽  
Insect Defensin

The regulated degradation of a 3-hydroxy-3-methylglutaryl-coenzyme A reductase reporter construct occurs in the endoplasmic reticulum

1994 ◽  
Vol 107 (9) ◽  
pp. 2635-2642
Author(s):  
L.W. Lecureux ◽  
B.W. Wattenberg
Keyword(s):  
Endoplasmic Reticulum ◽  
Coenzyme A ◽  
Cholesterol Biosynthesis ◽  
Mevalonic Acid ◽  
Dna Encoding ◽  
Hmg Coa Reductase ◽  
Steady State Levels ◽  
Coa Reductase ◽  
Membrane Anchoring ◽  
Beta Galactosidase

The rate-limiting enzyme in cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl-coenzyme A (HMG CoA) reductase, is regulated at a number of levels. One important mechanism is regulation of the half-life of the protein by a controlled proteolytic system. This comes about in response to downstream products of the sterol biosynthetic pathway. Little is known about this system, including where in the cell this regulated degradation occurs. HMG CoA reductase resides in the endoplasmic reticulum. To localize the site of regulated degradation of HMG CoA reductase, we used a construct that fuses the N-terminal membrane-anchoring domain of HMG CoA reductase in-frame with beta-galactosidase as a reporter domain (HM-Gal). HM-Gal has previously been shown to reproduce faithfully the degradative properties of native HMG CoA reductase (Chun et al. (1990) J. Biol. Chem. 265, 22004–22010). CHO cells transfected with DNA encoding HM-Gal were exposed to mevalonic acid, which enhances the rate of HMG CoA reductase degradation several fold, and leads to the reduction of the steady state levels of HM-Gal by 80–90%. To accumulate HMG CoA reductase at the site of degradation, cells were simultaneously treated with N-acetyl-leucyl-leucyl-norleucinal (ALLN), which inhibits the protease responsible for reductase degradation. HM-Gal was localized morphologically by immunofluorescence and biochemically by measuring beta-galactosidase activity in Percoll gradients of cellular homogenates. Using either technique HM-Gal localization was indistinguishable from that of ER markers in both control cells and in cells treated to accumulate HMG CoA reductase at the site of degradation.(ABSTRACT TRUNCATED AT 250 WORDS)

Characterization of the Luteinizing Hormone Beta (LH-β) Subunit Gene in the Goat

2021 ◽  
Author(s):  
Jakeer Husen A Olekar ◽  
Ashish Kumar ◽  
Ambika Sharma ◽  
Kranti Dev
Keyword(s):  
Luteinizing Hormone ◽  
Genomic Dna ◽  
Critical Role ◽  
Glycosylation Site ◽  
Restriction Enzyme Digestion ◽  
Β Subunit ◽  
Dna Encoding ◽  
Result Analysis ◽  
Cloned Gene

Background: Luteinizing hormone (LH) plays a critical role in ovulation and maintenance of pregnancy in female and gamete production in male during fertile phase of life. Physiological disturbance of this hormone leads to conditions like delayed ovulation, anovulation, cystic ovarian disease and lack of sexual desire in male. Since, there had been no report of molecular characterization of β-subunit of luteinizing hormone (LH) of Indian goat, the present study aimed to clone and characterize genomic DNA encoding LHβ subunit.Methods: Genomic DNA was extracted from goat blood and amplified using specific LHβ gene primers. After cloning and transformation, plasmids were isolated from randomly selected white colonies. Presence of insert was confirmed by restriction enzyme digestion of plasmids. After confirmation by PCR, plasmids were sent for DNA sequencing. Result: Analysis of sequence revealed an insert of 1006 bp size as expected. Comparison of nucleotide sequence revealed the cloned gene to be is LHβ encoding 141 amino acids. It showed 97.3 and 91.7% similarity with sheep and cattle respectively. Inferred amino acid sequence showed absolute similarity (100%) with sheep and buffalo. The common and essential features such as twelve cysteine molecules, a single potential N-glycosylation site, the CAGY region and another tetrapeptide CGPC are all found in the goat sequence too.

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