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Isolation and expression pattern of RGS21 gene, a novel RGS member

100%

Li X., Chen L., Ji C., Liu B., Gu J., Xu J., Zou X., Gu S., Mao Y.

2005

vol. 52

issue 4

943-946

Regulators of G-protein signaling (RGS) proteins are known for the RGS domain that is composed of a conserved stretch of 120 amino acids, which binds directly to activated G-protein α subunits and acts as a GTPase-activating protein (GAP), leading to their deactivation and termination of downstream signals. In this study, a novel human RGS cDNA (RGS21), 1795 bp long and encoding a 152-amino acid polypeptide, was isolated by large-scale sequencing analysis of a human fetal brain cDNA library. Unlike other RGS family members, RGS21 gene has no additional domain/motif and may represent the smallest known member of RGS family. It may belong to the B/R4 subfamily, which suggests that it may serve exclusively as a negative regulator of αi/o family members and/or αq/11. PCR analysis showed that RGS21 mRNA was expressed ubiquitously in the 16 tissues examined, implying general physiological roles.

Molecular cloning and expression analysis of a new gene for short-chain dehydrogenase/reductase 9

100%

Liu S., Huang C., Li D., Ren W., Zhang H., Qi M., Li X., Yu L.

2007

vol. 54

issue 1

213-218

We report here the cloning and characterization of a novel human short-chain dehydrogenases/reductase gene SCDR9, isolated from a human liver cDNA library, and mapped to 4q22.1 by browsing the UCSC genomic database. SCDR9 containing an ORF with a length of 900 bp, encoding a protein with a signal peptide sequence and an adh_short domain. GFP localization shows SCDR9 protein concentrated in some site of the cytoplasm, but not in the ER. Expression pattern in eighteen tissues revealed that SCDR9 is expressed highly in liver. Soluble recombinant protein was successfully purified from Escherichia coli using pET28A(+) expression vector. Our data provides important information for further study of the function of the SCDR9 gene and its products.

cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type VI.

81%

Zhang J., Dai J., Zhao E., Lin Y., Zeng L., Chen J., Zheng H., Wang Y., Li X., Ying K., Xie Y., Mao Y.

vol. 51

issue 4

1051-1058

Peptidylarginine deiminase (PAD) catalyzes the post-translational modification of protein through the conversion of arginine to citrulline in the presence of calcium ions. Human, similar to rodents, has four isoforms of PAD (type I, II, III and IV/V), each of which is distinct in substrate specificity and tissue specific expression. In our large-scale sequencing project, we identified a new human PAD cDNA from a human fetal brain cDNA library. The putative protein encoded by this cDNA is designated hPADVI. Expression analysis of hPADVI showed that it is mainly expressed in adult human ovary and peripheral blood leukocytes. We conclude that hPADVI may be orthologous to mouse ePAD, basing on sequence comparison, chromosome localization and exon-intron structure analysis. PAD-mediated deimination of epithelial cell keratin resulting in cytoskeletal remodeling suggests a possible role for hPADVI in cytoskeletal reorganization in the egg and in early embryo development. This study describes a new important member of the human PAD family.

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3 Acta Biochimica Polonica

1 2007

1 2005

1 2004

3 Li X.

2 Mao Y.

1 Chen J.

1 Chen L.

1 Dai J.

1 Gu J.

1 Gu S.

1 Huang C.

1 Ji C.

1 Li D.

1 Lin Y.

1 Liu B.

1 Liu S.

1 Qi M.

1 Ren W.

1 Wang Y.

1 Xie Y.

1 Xu J.

1 Ying K.

1 Yu L.

1 Zeng L.

1 Zhang H.

1 Zhang J.

1 Zhao E.

1 Zheng H.

1 Zou X.

Search results

Isolation and expression pattern of RGS21 gene, a novel RGS member

Molecular cloning and expression analysis of a new gene for short-chain dehydrogenase/reductase 9

cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type VI.