scholarly journals An alternatively spliced gene encoding a Y-box protein showing maternal expression and tissue-specific zygotic expression in the ascidian embryo

1998 ◽  
Vol 40 (6) ◽  
pp. 631-640
Author(s):  
Michiko R. Wada ◽  
Yoshiaki Ohtani ◽  
Yumiko Shibata ◽  
Kimio J. Tanaka ◽  
Naomi Tanimoto ◽  
...  
Keyword(s):  
Gene Encoding ◽  
Tissue Specific ◽  
Maternal Expression ◽  
Alternatively Spliced ◽  
Ascidian Embryo

An alternatively spliced gene encoding a Y-box protein showing maternal expression and tissue-specific zygotic expression in the ascidian embryo

1998 ◽  
Vol 40 (5) ◽  
pp. 631-640 ◽  
Author(s):  
Michiko R. Wada ◽  
Yoshiaki Ohtani ◽  
Yumiko Shibata ◽  
Kimio J. Tanaka ◽  
Naomi Tanimoto ◽  
...  
Keyword(s):  
Gene Encoding ◽  
Tissue Specific ◽  
Maternal Expression ◽  
Alternatively Spliced ◽  
Ascidian Embryo

Stable transfer and restricted expression of a cloned class I gene encoding a secreted transplantation-like antigen

1985 ◽  
Vol 5 (6) ◽  
pp. 1295-1300
Author(s):  
Y Barra ◽  
K Tanaka ◽  
K J Isselbacher ◽  
G Khoury ◽  
G Jay
Keyword(s):  
Molecular Mechanisms ◽  
Cell Types ◽  
Class I ◽  
Regulatory Sequences ◽  
Transcriptional Enhancer ◽  
Gene Encoding ◽  
Specific Expression ◽  
Tissue Specific ◽  
Functional Studies ◽  
I Gene

The identification of a unique major histocompatibility complex class I gene, designated Q10, which encodes a secreted rather than a cell surface antigen has led to questions regarding its potential role in regulating immunological functions. Since the Q10 gene is specifically activated only in the liver, we sought to define the molecular mechanisms which control its expression in a tissue-specific fashion. Results obtained by transfection of the cloned Q10 gene, either in the absence or presence of a heterologous transcriptional enhancer, into a variety of cell types of different tissue derivations are consistent with the Q10 gene being regulated at two levels. The first is by a cis-dependent mechanism which appears to involve site-specific DNA methylation. The second is by a trans-acting mechanism which would include the possibility of an enhancer binding factor. The ability to efficiently express the Q10 gene in certain transfected cell lines offers an opportunity to obtain this secreted class I antigen in quantities sufficient for functional studies; this should also make it possible to define regulatory sequences which may be responsible for the tissue-specific expression of Q10.

scholarly journals Stable transfer and restricted expression of a cloned class I gene encoding a secreted transplantation-like antigen.

1985 ◽  
Vol 5 (6) ◽  
pp. 1295-1300 ◽  
Author(s):  
Y Barra ◽  
K Tanaka ◽  
K J Isselbacher ◽  
G Khoury ◽  
G Jay
Keyword(s):  
Molecular Mechanisms ◽  
Cell Types ◽  
Class I ◽  
Regulatory Sequences ◽  
Transcriptional Enhancer ◽  
Gene Encoding ◽  
Specific Expression ◽  
Tissue Specific ◽  
Functional Studies ◽  
I Gene

The identification of a unique major histocompatibility complex class I gene, designated Q10, which encodes a secreted rather than a cell surface antigen has led to questions regarding its potential role in regulating immunological functions. Since the Q10 gene is specifically activated only in the liver, we sought to define the molecular mechanisms which control its expression in a tissue-specific fashion. Results obtained by transfection of the cloned Q10 gene, either in the absence or presence of a heterologous transcriptional enhancer, into a variety of cell types of different tissue derivations are consistent with the Q10 gene being regulated at two levels. The first is by a cis-dependent mechanism which appears to involve site-specific DNA methylation. The second is by a trans-acting mechanism which would include the possibility of an enhancer binding factor. The ability to efficiently express the Q10 gene in certain transfected cell lines offers an opportunity to obtain this secreted class I antigen in quantities sufficient for functional studies; this should also make it possible to define regulatory sequences which may be responsible for the tissue-specific expression of Q10.

Genomic Cloning, Physical Mapping, and Expression of Human Type 2 Cystatin Genes

1993 ◽  
Vol 4 (3) ◽  
pp. 573-580 ◽  
Author(s):  
D.P. Dickinson ◽  
M. Thiesse ◽  
L.D. Dempsey ◽  
S.J. Millar
Keyword(s):  
Gene Family ◽  
Cystatin C ◽  
Small Subset ◽  
Gene Encoding ◽  
Tandem Gene Duplication ◽  
Rnase Protection ◽  
Tissue Specific ◽  
Genes Encoding ◽  
Cystatin Gene

Humans carry one gene encoding cystatin C and six to eight genes with homology to an S-like cystatin hybridization probe. However, the precise composition and organization of the cystatin gene family remains to be established. Further, the pattern of tissue-specific expression has not been fully defined. We have previously shown that the type 2 cystatin genes are clustered together in a ca. 270 kb region (the CST locus). To determine the structure of this region, we have sought to clone the entire CST locus. Our approach has been to isolate cosmid and lambda genomic clones carrying cystatin genes and then to use "walk" probes derived from the end regions of these clones to identify other clones, which extend them. To date, we have obtained over 320 kb of distinct sequences. Based on restriction maps, sequencing, and hybridization analyses, we have identified eight apparently nonallelic copies of cystatin genes. These include one gene for cystatin C, four closely related genes encoding S-like cystatins, and three genes encoding relatively divergent sequences. Complete assembly of these clones into an unambiguous contiguous sequence is hampered by the presence of flanking locus-specific repetitive-like sequences. RNase protection assays used to characterize the tissue-specific patterns of expression showed that cystatin C is expressed at modest, comparable levels in all tissues examined, whereas expression of the CST 1 gene, encoding cystatin SA-I, was found to be restricted to a small subset of tissues, with the highest level in the submandibular gland. The cystatin gene family, therefore, appears to have evolved by tandem gene duplication, followed by the acquisition of control elements influencing the location and level of expression. The cystatin gene family is, thus, a potentially powerful system for the future study of mechanisms of gene regulation in human salivary glands.

scholarly journals Alternatively spliced mRNA variants of chloroplast ascorbate peroxidase isoenzymes in spinach leaves

1999 ◽  
Vol 338 (1) ◽  
pp. 41-48 ◽  
Author(s):  
Kazuya YOSHIMURA ◽  
Yukinori YABUTA ◽  
Masahiro TAMOI ◽  
Takahiro ISHIKAWA ◽  
Shigeru SHIGEOKA
Keyword(s):  
Ascorbate Peroxidase ◽  
Differential Splicing ◽  
Gene Encoding ◽  
S1 Nuclease ◽  
C Terminus ◽  
Mrna Variants ◽  
Alternatively Spliced ◽  
Splicing Efficiency ◽  
Spinach Leaves

We have previously shown that stromal and thylakoid-bound ascorbate peroxidase (APX) isoenzymes of spinach chloroplasts arise from a common pre-mRNA by alternative splicing in the C-terminus of the isoenzymes [Ishikawa, Yoshimura, Tamoi, Takeda and Shigeoka (1997) Biochem. J. 328, 795–800]. To explore the production of mature, functional mRNA encoding chloroplast APX isoenzymes, reverse transcriptase-mediated PCR and S1 nuclease protection analysis were performed with poly(A)+ RNA or polysomal RNA from spinach leaves. As a result, four mRNA variants, one form of thylakoid-bound APX (tAPX-I) and three forms of stromal APX (sAPX-I, sAPX-II and sAPX-III), were identified. The sAPX-I and sAPX-III mRNA species were generated through the excision of intron 11; they encoded the previously identified sAPX protein. Interestingly, the sAPX-II mRNA was generated by the insertion of intron 11 between exons 11 and 12. The use of this insertional sequence was in frame with the coding sequence and would lead to the production of a novel isoenzyme containing a C-terminus in which a seven-residue sequence replaced the last residue of the previously identified sAPX. The recombinant novel enzyme expressed in Escherichia coli showed the same enzymic properties (except for molecular mass) as the recombinant sAPX from the previously identified sAPX-I mRNA, suggesting that the protein translated from the sAPX-II mRNA is functional as a soluble APX in vivo. The S1 nuclease protection analysis showed that the expression levels of mRNA variants for sAPX and tAPX isoenzymes are in nearly equal quantities throughout the spinach leaves grown under normal conditions. The present results demonstrate that the expression of chloroplast APX isoenzymes is regulated by a differential splicing efficiency that is dependent on the 3´-terminal processing of ApxII, the gene encoding the chloroplast APX isoenzymes.

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