scholarly journals Primary Structure and Effect of pH on the Expression of the Plasma Membrane H+-ATPase from Dunaliella acidophila and Dunaliella salina

1996 ◽  
Vol 112 (4) ◽  
pp. 1693-1702 ◽  
Author(s):  
M. Weiss ◽  
U. Pick
Keyword(s):  
Plasma Membrane ◽  
Primary Structure ◽  
Dunaliella Salina ◽  
Effect Of Ph ◽  
Dunaliella Acidophila

scholarly journals Primary structure of rat plasma membrane Ca2+-ATPase isoform 4 and analysis of alternative splicing patterns at splice site A

1995 ◽  
Vol 306 (3) ◽  
pp. 779-785 ◽  
Author(s):  
T P Keeton ◽  
G E Shull
Keyword(s):  
Plasma Membrane ◽  
Alternative Splicing ◽  
Splice Site ◽  
Primary Structure ◽  
Sequence Divergence ◽  
Rat Plasma ◽  
Pcr Analysis ◽  
Rat Tissues ◽  
Mrna Tissue Distribution ◽  
Splicing Patterns

We have determined the primary structure of the rat plasma membrane Ca(2+)-ATPase isoform 4 (PMCA4), and have analysed its mRNA tissue distribution and alternative splicing patterns at splice site A. Rat PMCA4 (rPMCA4) genomic clones were isolated and used to determine the coding sequences and intron/exon organization of the 5′-end of the gene, and the remaining coding sequence was determined from PCR-amplified cDNA fragments. Pairwise comparisons reveal that the amino acid sequence of rPMCA4 has diverged substantially from those of rPMCA isoforms 1, 2 and 3 (73-76% identity) and from that of human PMCA4 (87%). Despite the high degree of sequence divergence between the two species, comparisons of intron and untranslated mRNA sequences with the corresponding human sequences confirm the identity of this rat isoform as PMCA4. Northern blot studies demonstrate that the PMCA4 mRNA is expressed in all rat tissues examined except liver, with the highest levels in uterus and stomach. A combination of PCR analysis of alternative splicing patterns and sequence analysis of the gene demonstrate that a 36 nt exon at site A is included in PMCA4 mRNAs of most tissues but is largely excluded in heart and testis. Alternative splicing of both the 36 nt exon and a previously characterized 175 nt exon at splice site C, each of which can be either included or excluded in a highly tissue-specific manner, leads to the production of four different PMCA4 variants ranging in size from 1157 to 1203 amino acids.

Lipid composition of the plasma-membrane of the halotolerant alga, Dunaliella salina

1986 ◽  
Vol 857 (2) ◽  
pp. 165-172 ◽  
Author(s):  
Meir Sheffer ◽  
Adina Fried ◽  
Hugo E. Gottlieb ◽  
Alisa Tietz ◽  
Mordhay Avron
Keyword(s):  
Plasma Membrane ◽  
Lipid Composition ◽  
Dunaliella Salina

Primary structure of the cAMP-dependent phosphorylation site of the plasma membrane calcium pump

Biochemistry ◽  
1989 ◽  
Vol 28 (10) ◽  
pp. 4253-4258 ◽  
Author(s):  
Peter H. James ◽  
Martin Pruschy ◽  
Thomas E. Vorherr ◽  
John T. Penniston ◽  
Ernesto Carafoli
Keyword(s):  
Plasma Membrane ◽  
Primary Structure ◽  
Phosphorylation Site ◽  
Calcium Pump ◽  
Plasma Membrane Calcium Pump

scholarly journals Effect of osmotic shock on the redox system in plasma membrane of Dunaliella salina

Cell Research ◽  
1996 ◽  
Vol 6 (1) ◽  
pp. 31-38 ◽  
Author(s):  
Si Xue Chen ◽  
Chi Chiong Yen ◽  
Xin Zhi Jiao
Keyword(s):  
Plasma Membrane ◽  
Dunaliella Salina ◽  
Osmotic Shock ◽  
Redox System

scholarly journals Complete primary structure of a human plasma membrane Ca2+ pump.

1988 ◽  
Vol 263 (28) ◽  
pp. 14152-14159 ◽  
Author(s):  
A K Verma ◽  
A G Filoteo ◽  
D R Stanford ◽  
E D Wieben ◽  
J T Penniston ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Human Plasma ◽  
Primary Structure ◽  
Complete Primary Structure
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