scholarly journals Nucleotide sequence of a rabbit genomic DNA encoding mature endothelin-3

1990 ◽  
Vol 18 (2) ◽  
pp. 374-374 ◽  
Author(s):  
Shoichi Ohkubo ◽  
Yasuaki Itoh ◽  
Chiharu Kimura ◽  
Haruo Onda ◽  
Masahiko Fujino
1993 ◽  
Vol 57 (1) ◽  
pp. 131-133 ◽  
Author(s):  
Shinya Kawai ◽  
Yasuo Matsumoto ◽  
Shinya Kajita ◽  
Keiko Yamada ◽  
Yoshihiro Katayama ◽  
...  

1995 ◽  
Vol 107 (4) ◽  
pp. 1453-1453 ◽  
Author(s):  
H. Y. Oh ◽  
M. S. Yang

1996 ◽  
Vol 318 (2) ◽  
pp. 689-699 ◽  
Author(s):  
Leonard DODE ◽  
Frank WUYTACK ◽  
Patrick F. J. KOOLS ◽  
Fouzia BABA-AISSA ◽  
Luc RAEYMAEKERS ◽  
...  

cDNA and genomic clones encoding human sarco/endoplasmic reticulum Ca2+-ATPase 3 (SERCA3) were isolated. The composite nucleotide sequence of the 4.6 kb cDNA, as well as the partial structure of 25 kb of genomic DNA encoding all but the 5´ region of the gene, was determined. The nucleotide sequence coding for the last six amino acids of the pump and the 3´-untranslated region were identified within the sequence of the last exon. Northern blot hybridization analysis using cDNA probes derived from this exon detected a 4.8 kb transcript in several human tissues. Using a cDNA probe derived from the 5´-coding region an unexpected mRNA distribution pattern, consisting of two mRNA species of 4.8 and 4.0 kb, was detected in thyroid gland and bone marrow only. This is the first indication of an alternative splicing mechanism operating on the SERCA3 gene transcript, which most likely generates SERCA3 isoforms with altered C-termini. Human SERCA3 expressed in platelets and in COS cells transfected with the corresponding cDNA was detected with the previously described antibody N89 (directed against the N-terminal region of rat SERCA3) and with a new SERCA3-specific antiserum C91, directed against the extreme C-terminus of the human isoform. A monoclonal antibody PL/IM430, previously assumed to recognize SERCA3 in human platelets, does not react with the 97 kDa human SERCA3 transiently expressed in COS cells. Therefore the 97 kDa isoform detected by PL/IM430 more likely represents a novel SERCA pump, as recently suggested [Kovács, Corvazier, Papp, Magnier, Bredoux, Enyedi, Sarkadi and Enouf (1994) J. Biol. Chem. 269, 6177–6184]. Finally, by fluorescence in situ hybridization and chromosome G-banding analyses, the SERCA3 gene was assigned to human chromosome 17p13.3.


2006 ◽  
Vol 188 (3) ◽  
pp. 1039-1048 ◽  
Author(s):  
Ellen T. O'Connor ◽  
Andrzej Piekarowicz ◽  
Karen V. Swanson ◽  
J. McLeod Griffiss ◽  
Daniel C. Stein

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.


FEBS Letters ◽  
1991 ◽  
Vol 283 (1) ◽  
pp. 27-32 ◽  
Author(s):  
Javier Bordallo ◽  
Carmen Bordallo ◽  
Gascón Santiago ◽  
Paz Suárez-Rendueles

1992 ◽  
Vol 281 (3) ◽  
pp. 703-708 ◽  
Author(s):  
H Takeuchi ◽  
Y Shibano ◽  
K Morihara ◽  
J Fukushima ◽  
S Inami ◽  
...  

The DNA encoding the collagenase of Vibrio alginolyticus was cloned, and its complete nucleotide sequence was determined. When the cloned gene was ligated to pUC18, the Escherichia coli expression vector, bacteria carrying the gene exhibited both collagenase antigen and collagenase activity. The open reading frame from the ATG initiation codon was 2442 bp in length for the collagenase structural gene. The amino acid sequence, deduced from the nucleotide sequence, revealed that the mature collagenase consists of 739 amino acids with an Mr of 81875. The amino acid sequences of 20 polypeptide fragments were completely identical with the deduced amino acid sequences of the collagenase gene. The amino acid composition predicted from the DNA sequence was similar to the chemically determined composition of purified collagenase reported previously. The analyses of both the DNA and amino acid sequences of the collagenase gene were rigorously performed, but we could not detect any significant sequence similarity to other collagenases.


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

Sign in / Sign up

Export Citation Format

Share Document