Human proα1(I) collagen gene structure reveals evolutionary conservation of a pattern of introns and exons

Chu, Mon‐Li; Wet, W de; Bernard, Michael P.; Ding, Jixiang; Morabito, Maria A.; Myers, Jeanne C.; Williams, Charlene J.; Ramirez, Francesco

doi:10.1038/310337a0

Cited by 197 publications

(73 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The insert of 14 amino acids in CR4 after the Cxi2 spacer can itself be aligned with the four Cxi2 spacer sequences, suggesting that this region of the CR4 repeat may have arisen by a short tandem duplication. Abbreviations for aligned proteins are (HPC) Human pro-alpha-1 (I) collagen (Chu et al 1984); (MTSP2) mouse thrombospondin 2 (Bomstein et al 1991); (von Wlbrd) von Willebrand factor (Verweij et al 1986); (R-Slam) rat S-laminin (Hunter et al 1989); (Sas2) second repeat (of four) of the predicted Diosophila stranded at second [sas] gene product (Schonbaum et al 1992); (CEF-10) CEF-10 (Simmons et al 1989). (D) Sequence alignment of the three SR repeats (SR1-SR3).…”

Section: Genes and Development 2611mentioning

confidence: 99%

Dorsal-ventral patterning of the Drosophila embryo depends on a putative negative growth factor encoded by the short gastrulation gene.

Vincent¹,

Solloway²,

O’Neill³

et al. 1994

Genes Dev.

295

232

View full text Add to dashboard Cite

Pattern lormation in the dorsal region of the Drosophila embryo depends on the activity of a small group of zygotically acting genes, dpp, a key gene in this group, encodes a TGF-p-like product (Dpp) that has been proposed to function as a morphogen with peak levels of Dpp-specifying amnioserosa, the dorsal-most cell type, and lower Dpp levels specifying dorsal ectoderm. The short gastrulation gene also contributes to patterning the dorsal region, but unlike the other genes involved in this process, sog activity is only required in ventral cells. Genetic evidence indicates that sog functions to antagonize dpp activity. In this report we present further phenotypic characterization of sog mutant embryos in dorsal and lateral regions and describe the cloning of the sog locus, sog is expressed in a broad lateral stripe of cells that abuts the dorsal territory of dfpp-expressing cells, sog is predicted to encode a protein with an internal signal sequence and a large extracellular domain containing four repeats of a novel motif defined by the spacing of 10 cysteine residues that is distantly related to domains present in thrombospondin and procollagen. We propose that one or more of these cysteine repeats can be liberated by proteolytic cleavage of the primary Sog protein. These putative soluble Sog peptides may then diffuse into the dorsal region to antagonize the activity of Dpp, leading to the subdivision of the dorsal territory into amnioserosa and dorsal ectoderm.[

show abstract

Section: Genes and Development 2611mentioning

confidence: 99%

Dorsal-ventral patterning of the Drosophila embryo depends on a putative negative growth factor encoded by the short gastrulation gene.

Vincent¹,

Solloway²,

O’Neill³

et al. 1994

Genes Dev.

295

232

View full text Add to dashboard Cite

show abstract

“…The observation of a very large (probably 18,000 to 20,000 bases) al(I) collagen RNA in transformed chondrocytes was somewhat surprising; such a large al(I) collagen RNA has never been observed in any other cell type. Since the human al(I) collagen gene is 18,000 base pairs in size (9), this very large RNA may represent a primary transcript of the al(I) collagen gene. Its presence would imply that, although the processing of al(I) collagen RNA in transformed chondrocytes is similar to that in fibroblasts, it may be less efficient.…”

mentioning

confidence: 99%

Control of types I and II collagen and fibronectin gene expression in chondrocytes delineated by viral transformation.

Allebach¹,

Boettiger²,

Pacifici³

et al. 1985

Mol. Cell. Biol.

View full text Add to dashboard Cite

We have analyzed the effects of transformation by Rous sarcoma virus on expression of types I and II collagen and fibronectin genes in vertebral chondrocytes and compared them with expression of these genes in skin fibroblasts. Transformed chondrocytes display a dramatically decreased amount of type II collagen RNA, which can account fully for the decreased synthetic rate of this protein. Paradoxically, these cells also display greatly increased amounts of type I collagen RNAs, which are translated efficientlv in vitro, but not in the intact cells. We show here that the type I collagen RNAs in transformed chondrocytes are nearly indistinguishable from those found in skin fibroblasts, and that they clearly differ from the type I collagen RNAs found in normal chondrocytes. Transformed chondrocytes also display an increased amount of fibronectin RNA, which can account fully for the increased synthetic rate of this protein. Thus, the effects of transformation by Rous sarcoma virus on type I collagen and fibronectin RNAs in chondrocytes are the opposite of those observed in fibroblasts, which display decreased amounts of these three RNAs. These data indicate that the effects of transformation on the genes encoding type I collagen and fibronectin must be modulated by host cell-specific factors. They also imply that the types I and II collagen genes may be regulated by different mechanisms, the type I genes being controlled at both transcriptional and posttranscriptional levels, and the type II gene being controlled primarily at the transcriptional level.Transformation of differentiated cells by tumor viruses has provided a useful tool for analyzing the mechanisms of cellular gene expression. This has been particularly true for the genes encoding extracellular matrix proteins, whose expression is decreased by transformation with certain viruses. For example, transformation of chicken embryo fibroblasts by Rous sarcoma virus (RSV) results in reduced synthesis of type I collagen (10,20,25,(45)(46)(47) and, in some cases, fibronectin (36,39). Similarly, transformation of chicken vertebral chondrocytes by RSV results in decreased synthesis of type II collagen and the major cartilage proteoglycan (2,18,37,38). The reduced rates of synthesis of type I collagen and fibronectin in transformed fibroblasts reflect decreased amounts of the corresponding RNAs (1, 3. 15,19,43,45,46,51) These data demonstrate that transformation by RSV has opposite effects on the expression of type I collagen and fibronectin genes in chondrocytes and fibroblasts and imply that the action of src is modulated by host cell factors that differ between these cell types. They also imply that the types I and II collagen genes may be regulated by different mechanisms. The genes encoding type I collagen, a protein which is synthesized by many cell types, appear to be regulated at both transcriptional and posttranscriptional levels. In contrast, the type II collagen gene, which is expressed only by a very limited number of terminally differentiated cell type...

show abstract

“…It is clear that the codon splits between exon 1 and exon 2 and an extra base was also found at the 3' end of exon 1 by Nunez et al [20]. Split codons also occur between exon 1 and 2 of the human procollagen 12(I) gene [21,22], and between exons…”

Section: Split Codonmentioning

confidence: 93%

Genomic organization of the human procollagen α1 (II) collagen gene

Huang

Seyer

Thompson

et al. 1991

European Journal of Biochemistry

View full text Add to dashboard Cite

The nucleotide sequence of the human procollagen a1 (11) collagen gene extending from within the first intron through exon 15, and part of the 15th intron has been determined. This sequence analysis (7056 bases) identifies the intron/exon organization of the region of this gene encoding the N-propeptide and part of the triple-helical domain. Structural comparison of this with the genes of other human fibrillar collagens shows considerable diversity in terms of size and number of introns and exons that encodes the N-propeptide domain. Although the genomic structure of the human procollagen al(I1) gene is quite different from the rat procollagen al(1I) gene, the nucleotide coding sequences are 89% identical.Type I1 collagen is the major structural component of cartilage. It represents a genetically distinct member of fibrillar collagen family and is comprised of three identical aI(11) chains [l -31. Fibrillar procollagens are synthesized in precursor forms containing propeptides at both the amino and carboxyl ends of the molecules. Propeptides are thought to be involved in alignment of the three procollagens chains during triple-helix formation and in their secretion [l -31. Propeptides are cleaved after secretion of the native type I1 collagen molecule [l -31. This process and the coordinated expression of collagen genes are vitally important during vertebrate development [4]. Recently, genetic lesions in the procollagen al(I1) gene have been identified as the basis of several human diseases [5 -81.The human procollagen al(I1) gene has been isolated and characterized using a cosmid clone and a series of overlapping genomic clones [8, 91. The entire gene spans six large EcoRI fragments with sizes of 4.8, 7.3, 5.2, 9.2, 3.7 and 4.3 kb in the order of 5' end to 3' end of the gene. The nucleotide sequence of the 3' region of the gene encoding the C-propeptide has been determined [9]. Recently, overlapping cDNA clones encoding the complete helical region of the human procollagen al(I1) gene were isolated and identified [5]. Analysis of the cDNAs revealed the nucleotide sequence of the mRNA and the deduced amino acid sequence. Exons in the triple-helical and the C-propeptide region of human type I1 collagen are identical in size to exons of the chicken gene [ intronic structure in the triple-helical and the N-propeptide region has not been fully identified [12, 131. In this study, we present genomic nucleotide sequence of 6885 residues of the human procollagen a1 (11) gene encoding the 3' end of the first intron continuously through the 5' end of the 15th intron. This area covers the complete N-propeptide (except exon I) and residues 1-272 of the triple-helical domain of this gene. This information, for the first time, identified the genomic organization of the human type I1 collagen gene. Structural comparison of this gene with other human fibril-forming collagen genes and the rat type I1 collagen gene is presented. MATERIALS AND METHODS PlusmidThe 7.3-kb and 9.2-kb EcoRI fragments containing portions of the human ...

show abstract

Human proα1(I) collagen gene structure reveals evolutionary conservation of a pattern of introns and exons

Cited by 197 publications

References 19 publications

Dorsal-ventral patterning of the Drosophila embryo depends on a putative negative growth factor encoded by the short gastrulation gene.

Dorsal-ventral patterning of the Drosophila embryo depends on a putative negative growth factor encoded by the short gastrulation gene.

Control of types I and II collagen and fibronectin gene expression in chondrocytes delineated by viral transformation.

Genomic organization of the human procollagen α1 (II) collagen gene

Contact Info

Product

Resources

About