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Cloning and expression of a Nostoc sp. leucine biosynthetic gene in Escherichia coli (1986)

Cangelosi, Gerard A. ; Joseph, Cecillia M. ; Rosen, Joanne J. ; [et al.]

Springer

Archives of microbiology 145 (1986), S. 315-321

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ISSN: 1432-072X

Keywords: Cyanobacteria ; DNA restriction and cloning ; Gene fusions ; Leucine biosynthesis ; Mutant complementation ; Nostoc ; Transcription

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Genomic DNA extracted from the symbiotically-competent, heterocyst-forming cyanobacterium Nostoc sp. strain 7801 was resistant to cleavage by a number of restriction endonucleases. A cosmid library of Nostoc DNA was prepared and maintained in the modification-limited Escherichia coli strain HB101. Analysis of cloned Nostoc DNA fragments indicated infrequent occurrence of restriction endonuclease recognition sites in the Nostoc genome. The Nostoc genomic library was screened for sequences complementing mutations in the E. coli leucine and proline biosynthetic operons. Two cosmids complementing leuB were isolated but none for leuA, leuC, leuD, or proA were detected in 1000 cosmids. A 3.0 kb fragment subcloned from one of the cosmids complemented mutations in leuB when inserted into the HindIII site of pBR322 in either orientation, demonstrating that transcription of leuB originated within the cloned fragment. The cloned fragment also carries a second site capable of initiating transcription of fused antibiotic resistance genes. While transcription of Nostoc DNA sequences did occur in E. coli, unknown barriers must also exist that prevented additional biological complementation of specific E. coli mutations.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00470864

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Localization of basic fibroblast growth factor to the developing capillaries of the bovine retina (1989)

Hanneken, Anne ; Lutty, Gerard A. ; McLeod, D. Scott ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Journal of Cellular Physiology 138 (1989), S. 115-120

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ISSN: 0021-9541

Keywords: Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: The basic fibroblast growth factor (FGF) is a potent mitogen that has vascular endothelium as one of its principle target cells. Recent work has provided both the complete amino acid sequence of basic FGF and the nucleotide sequence of the genes for both human and bovine basic FGF. Although capillary endothelial cells have been shown to produce basic FGF in vitro and to deposit basic FGF in their extracellular matrix in vitro as well, no direct evidence yet exists for the distribution of basic FGF in vivo. Antipeptide antibodies were prepared against a 15-amino-acid sequence from the amino terminus of basic FGF in order to avoid cross-reactivity with acidic FGF, a protein with 55% overall homology to basic FGF. After affinity purification, these antisera were used to localize the basic fibroblast growth factor in the fetal and adult bovine retina. Immunoreactive material was found in capillaries of the inner nuclear layer, a capillary network undergoing development during the third trimester in the fetal bovine eye. Although the resolution of the technique does not permit a unique assignment of cellular localization, the presence of stain immediately adjacent to the lumen of capillaries suggests that capillary endothelial cells may produce the basic fibroblast growth factor in vivo during vascular development.

Additional Material: 6 Ill.