Analysis of the mouse γ-crystallin gene family: assignment of multiple cDNAs to discrete genomic sequences and characterization of a representative gene

Lok, Si; Tsui, Lap‐Chee; Shinohara, Toshimichi; Piatigorsky, Joram; Gold, R; Breitman, Martin L.

doi:10.1093/nar/12.11.4517

Cited by 68 publications

(52 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, as in those proteins, it probably comprises a globular domain with an internal 2-fold symmetry axis relating the two motifs. In ycrystallin too, one domain, containing a 2-fold repeat, is coded in one exon [22,28]. These repeated units are considerably shorter than the predicted &-like motifs described above [ 12-141. Exons 2 and 3 contain the region of homology described by Ingolia and Craig [S] (residues 72-145).…”

Section: Gene and Protein Structurementioning

confidence: 99%

Domain structure and evolution in α‐crystallins and small heat‐shock proteins

Wistow

1985

FEBS Letters

164

View full text Add to dashboard Cite

Section: Gene and Protein Structurementioning

confidence: 99%

Domain structure and evolution in α‐crystallins and small heat‐shock proteins

Wistow

1985

FEBS Letters

164

View full text Add to dashboard Cite

“…Our previous gel-blot hybridization analyses revealed at least five different -y-crystallin genes within the mouse genome (26). Using mouse y-cDNAs (5,49), as probes, we isolated several K phage clones from a X47.1 phage DBA/2 mouse genomic library (25).…”

Section: )mentioning

confidence: 99%

“…Using mouse y-cDNAs (5,49), as probes, we isolated several K phage clones from a X47.1 phage DBA/2 mouse genomic library (25). The DNA sequence of one of the mouse y-crystallin genes, y4, has been reported previously (26). However, for reasons that will become clear below, we chose another mouse -y-crystallin gene, designated as -y2, for the present gene expression study.…”

Section: )mentioning

confidence: 99%

Lens-specific promoter activity of a mouse gamma-crystallin gene.

Lok¹,

Breitman²,

Chepelinsky³

et al. 1985

Mol. Cell. Biol.

View full text Add to dashboard Cite

Crystallins are the major water-soluble proteins in vertebrate eye lenses. These lens-specific proteins are encoded by several gene families, and their expression is differentially regulated during lens cell differentiation.Here we show that a cloned mouse y-crystallin promoter is active in lens explants derived from 14-day-old chicken embryos but inactive in a variety of cells of nonlens origin. We also show that sequences required for proper utilization of this promoter are contained between nucleotide positions -392 and +47 relative to the transcription initiation site; deletion of sequences from positions -392 to -171 completely abolishes promoter activity. Since chickens do not have y-crystallin genes, the expression of a mouse y-crystallin promoter in chicken lens cells suggests that different classes of crystallin genes may be regulated by common lens tissue-specific mechanism(s) independent of species.In mammals, development of the lens is accompanied by the appearance of three major classes of lens-specific proteins known as the a-, ,3-, and y-crystallins (for a review, see references 8 and 21). These water-soluble proteins are encoded by several gene families whose expression is tightly regulated during lens cell differentiation (39, 40). The present study concerns the -y-crystallins which are found exclusively in the terminally differentiated lens fiber cells (36). These antigenically related polypeptides exist as monomers with apparent molecular masses ranging from 20 to 25 kilodaltons. Although they are highly conserved in evolution, their complexity varies among different species. In the mouse lens, a total of six to seven different -y-crystallin polypeptides have been detected by two-dimensional gel electrophoresis (12).Although little is known about regulation of the -ycrystallin genes, the relationship between their expression and fiber cell elongation has long been the focus of investigation of lens cell differentiation (4, 37). In addition, the synthesis of different -y-crystallin polypeptides appears to be regulated in an age-related fashion (21). As predicted from the known three-dimensional structure determined for the major y-crystallin of the calf lens (3, 59), the different y-crystallin polypeptides appear to have slighly different surface properties which might be important for the shortrange ordering of macromolecules within the fiber cells (5, 9).Through molecular cloning and nucleotide sequence analysis of y-crystallin genes in the rats, mice, and humans (26, 29a, 31), it has become clear that the y-crystallin genes are highly homologous in structure. Each gene contains a small 5' exon encoding three amino acids followed by two major exons of approximately equal size, corresponding exactly to the two globular domains of the protein. While the coding sequences of the different -y-crystallin genes are highly conserved, the noncoding and intervening sequences have generally diverged. The first intron varies from 80 to 110 base pairs (bp) in length while the second ranges from 850 bp to...

show abstract

“…In the otA-crystallin gene, the 5' flanldng sequence of the mouse (8) and hamster (10) is highly conserved; however, much of this similarity is lost in the chicken (21). In the mouse, rat, and human y-crystallin gene family there are several sequences upstream from the TATA box that are highly conserved (19,(22)(23)(24)(25). Except for the 81-crystallin gene (26,27), no other crystallin gene contains the 5'CCAAT3' sequence in their 5' flanking region (5,8,10,19,(22)(23)(24)(25)(28)(29)(30).…”

Section: Introductionmentioning

confidence: 99%

“…In the mouse, rat, and human y-crystallin gene family there are several sequences upstream from the TATA box that are highly conserved (19,(22)(23)(24)(25). Except for the 81-crystallin gene (26,27), no other crystallin gene contains the 5'CCAAT3' sequence in their 5' flanking region (5,8,10,19,(22)(23)(24)(25)(28)(29)(30). The CCAAT sequence has been found to interact with a specific trans-acting factor (31)(32)(33).…”

Section: Introductionmentioning

confidence: 99%

Crystallin genes: lens specificity of the murine alpha A-crystallin gene.

Chepelinsky

Khillan

Mahon

et al. 1987

Environ Health Perspect

View full text Add to dashboard Cite

The abundant soluble proteins of the eye lens, the crystallins, are encoded by several gene families which are developmentally regulated in the embryonic lens. We have studied the expression of the murine aA-crystallin gene. Transfection experiments using the pSVO-CAT vector and explanted lens epithelia from embryonic chickens demonstrated proximal (-88 to -60) and distal (-111 to -85) regulatory sequences which interact when the aA-crystallin promoter is activated in the lens cells. Transgenic mouse experiments showed that the sequence between positions -366 to + 46 of the aA-crystallin promoter can drive foreign genes selectively in the lens. A fusion gene consisting of this aA-crystallin promoter sequence and the T-antigen gene of SV40 produced a lens tumor in transgenic mice. Thus, crystallin promoters provide a useful model for tissue-specific gene expression and permit targeting the expression of foreign genes to a highly differentiated tissue during development.

show abstract

Analysis of the mouse γ-crystallin gene family: assignment of multiple cDNAs to discrete genomic sequences and characterization of a representative gene

Cited by 68 publications

References 24 publications

Domain structure and evolution in α‐crystallins and small heat‐shock proteins

Domain structure and evolution in α‐crystallins and small heat‐shock proteins

Lens-specific promoter activity of a mouse gamma-crystallin gene.

Crystallin genes: lens specificity of the murine alpha A-crystallin gene.

Contact Info

Product

Resources

About