Functional role of positively charged amino acid residues in the transmembrane segments of the yeast PMA1 ATPase

1998 ◽  
Vol 43 (2) ◽  
pp. 208-210 ◽  
Author(s):  
K. P. Padmanabha ◽  
V. V. Petrov ◽  
C. W. Slayman
Keyword(s):  
Amino Acid ◽  
Functional Role ◽  
Amino Acid Residues ◽  
Transmembrane Segments ◽  
Positively Charged

scholarly journals Functional role of polar amino acid residues in Na+/H+ exchangers

2001 ◽  
Vol 357 (1) ◽  
pp. 1 ◽  
Author(s):  
Christine A. WIEBE ◽  
Emily R. DiBATTISTA ◽  
Larry FLIEGEL
Keyword(s):  
Amino Acid ◽  
Functional Role ◽  
Amino Acid Residues ◽  
Polar Amino Acid

The Functional Role of Positively Charged Amino Acid Side Chains in α-Bungarotoxin Revealed by Site-Directed Mutagenesis of a His-Tagged Recombinant α-Bungarotoxin†

Biochemistry ◽  
1999 ◽  
Vol 38 (24) ◽  
pp. 7847-7855 ◽  
Author(s):  
Julie A. Rosenthal ◽  
Mark M. Levandoski ◽  
Belle Chang ◽  
Jerald F. Potts ◽  
Qing-Luo Shi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Functional Role ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Side Chains ◽  
Amino Acid Side Chains ◽  
Positively Charged

scholarly journals Role of Amino Acid Residues in Transmembrane Segments IS6 and IIS6 of the Na+Channel α Subunit in Voltage-dependent Gating and Drug Block

2002 ◽  
Vol 277 (38) ◽  
pp. 35393-35401 ◽  
Author(s):  
Vladimir Yarov-Yarovoy ◽  
Jancy C. McPhee ◽  
Diane Idsvoog ◽  
Caroline Pate ◽  
Todd Scheuer ◽  
...  
Keyword(s):  
Amino Acid ◽  
Na Channel ◽  
Amino Acid Residues ◽  
Α Subunit ◽  
Transmembrane Segments ◽  
Voltage Dependent

scholarly journals Molecular characterization, tissue expression and polymorphisms of buffalo <i>PPARGC1A</i> gene

2020 ◽  
Vol 63 (2) ◽  
pp. 249-259
Author(s):  
Lihua Qiu ◽  
Xinyang Fan ◽  
Yongyun Zhang ◽  
Xiaohong Teng ◽  
Yongwang Miao
Keyword(s):  
Mammary Gland ◽  
Amino Acid ◽  
Milk Fat ◽  
Functional Role ◽  
Transmembrane Domain ◽  
Tissue Expression ◽  
River Buffalo ◽  
Nucleotide Polymorphisms ◽  
Amino Acid Residues

Abstract. PPARGC1A exerts important functions in activating many nuclear receptors and transcription factors that are related to energy balance. Previous studies have shown that PPARGC1A gene is associated with lactation traits of dairy cattle. However, the functional role of the buffalo PPARGC1A gene is still unknown. In this work, the complete coding sequence (CDS) of buffalo PPARGC1A was isolated and characterized for swamp and river buffalo. The CDS length of PPARGC1A for both types of buffalo was the same, which was composed of 2394 nucleotides and encoded a peptide composed of 797 amino acid residues. This protein belonged to a hydrophilic protein and contained one RRM_PPARGC1A domain (AA 674–764) without a signal peptide or a transmembrane domain. The differential expressions of this gene in 10 buffalo tissues in lactation and non-lactation displayed that the PPARGC1A was highly expressed in the muscle, heart, liver, brain and kidney of both non-lactating and lactating periods, but its expression was significantly different in the muscle, heart, liver, small intestine, mammary gland, rumen, spleen and lung between the two periods. Eight single nucleotide polymorphisms (SNPs) were found in buffalo, in which the c.778C>T, c.1257G>A and c.1311G>A were shared by two types of buffalo with similar allele frequencies, while the c.419C>T, c.759A>G, c.920C>A, c.926G>A and c.1509A>T were only observed in river buffalo. The SNP419, SNP920 and SNP926 were non-synonymous, which led to the amino acid changes of p.Ser140Phe, p.Pro307His and p.Arg309Lys. Seven nucleotide differential sites were identified in the PPARGC1A gene between buffalo and other Bovidae species. Phylogenetic analysis indicated that buffaloes were independently clustered into one branch, but they were closely related to the species of the Bos genus. The results indicate that buffalo PPARGC1A is an inducible transcriptional coactivator involved in regulating carbohydrate and fat metabolism. It can exert a functional role in a variety of buffalo tissues and may participate in milk fat synthesis and development in the mammary gland.

Functional roles of cationic amino acid residues in the sodium-dicarboxylate cotransporter 3 (NaDC-3) from winter flounder

2006 ◽  
Vol 291 (6) ◽  
pp. F1224-F1231 ◽  
Author(s):  
Yohannes Hagos ◽  
Jürgen Steffgen ◽  
Ahsan N. Rizwan ◽  
Denis Langheit ◽  
Ariane Knoll ◽  
...  
Keyword(s):  
Amino Acid ◽  
Transmembrane Helix ◽  
Site Directed Mutagenesis ◽  
Amino Acid Residues ◽  
Cationic Amino Acid ◽  
Functional Roles ◽  
Inward Currents ◽  
Induced Currents ◽  
Positively Charged

In the present study, we determined the functional role of 15 positively charged amino acid residues at or within 1 of the predicted 11 transmembrane helixes of the flounder renal sodium-dicarboxylate cotransporter fNaDC-3. Using site-directed mutagenesis, histidine (H), lysine (K), and arginine (R) residues of fNaDC-3 were replaced by alanine (A), isoleucine (I), or leucine (L). Most mutants showed sodium-dependent, lithium-inhibitable [14C]succinate uptake and, in two-electrode voltage-clamp (TEVC) experiments, Km and Δ Imax values comparable to wild-type (WT) fNaDC-3. The replacement of R109 and R110 by alanine and isoleucine (RR109/110AI) prevented the expression of fNaDC-3 at the plasma membrane. When the lysines at positions 232 and 235 were replaced by isoleucine (KK232/235II), the transporter was expressed but showed small transport rates and succinate-induced currents. K114I, located within transmembrane helix 4, showed [14C]succinate uptake similar to WT but relatively small inward currents. When K114 was replaced by arginine, glutamic acid (E), or glutamine (Q), all mutants were expressed at the cell surface. In [14C]succinate uptake and TEVC experiments performed simultaneously on the same oocytes, uptake was similar to or higher than WT, whereas succinate-induced currents were either comparable (K114R) to, or considerably smaller (K114E, K114I, K114Q) than, those evoked by WT. These results suggest that a positively charged residue at position 114 is required for electrogenic sodium-dicarboxylate cotransport.

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