Intermolecular hybridization of 5S rRNA with 18S rRNA: Identification of a 5′-terminally-located nucleotide sequence in mouse 5S rRNA which base-pairs with two specific complementary sequences in 18S rRNA

The nucleotide sequence of approx. 3 kilobases including the regulatory region, a non-coding exon and the first protein-coding exon from mouse lactate dehydrogenase-A (LDH-A) gene has been determined. The putative initiation sites of transcription and translation were deduced by comparing the nucleotide sequence of mouse LDH-A gene with those of a mouse LDH-A processed pseudogene and the LDH-A full-length cDNAs from rat and human. The tentative TATA and CAAT boxes, and the hexanucleotides CCGCCC have been identified. The sequence of AAATCTTGCTCAA of mouse LDH-A gene has also been found to show striking homology to the cyclic AMP-responsive sequences of eukaryotic genes regulated by cyclic AMP. It has been reported previously that the protein-coding sequence of mouse LDH-A gene is interrupted by six introns and the 3′ untranslated sequence of 485 nucleotides is not interrupted [Li, Tiano, Fukasawa, Yagi, Shimiza, Sharief, Nakashima & Pan (1985) Eur. J. Biochem. 149, 215-225]. An additional intron of 1653 base-pairs was found in the 5′ untranslated sequence of 101 nucleotides at 24 nucleotides upstream to the translation start site. Thus, mouse LDH-A gene containing seven introns spans approx. 11 kilobases and its length of mature mRNA is 1582 nucleotides, excluding the poly(A) tail.

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U14 base-pairs with 18S rRNA: a novel snoRNA interaction required for rRNA processing.

Genes & Development ◽

10.1101/gad.9.19.2433 ◽

1995 ◽

Vol 9 (19) ◽

pp. 2433-2443 ◽

Cited By ~ 66

Author(s):

W Q Liang ◽

M J Fournier

Keyword(s):

18S Rrna ◽

Rrna Processing ◽

Base Pairs

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Ribosomal shunting mediated by a translational enhancer element that base pairs to 18S rRNA

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.0603597103 ◽

2006 ◽

Vol 103 (25) ◽

pp. 9488-9493 ◽

Cited By ~ 39

Author(s):

S. A. Chappell ◽

J. Dresios ◽

G. M. Edelman ◽

V. P. Mauro

Keyword(s):

18S Rrna ◽

Base Pairs ◽

Enhancer Element ◽

Translational Enhancer

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RAD3 gene of Saccharomyces cerevisiae: nucleotide sequence of wild-type and mutant alleles, transcript mapping, and aspects of gene regulation

Molecular and Cellular Biology ◽

10.1128/mcb.5.1.17-26.1985 ◽

1985 ◽

Vol 5 (1) ◽

pp. 17-26

Author(s):

L Naumovski ◽

G Chu ◽

P Berg ◽

E C Friedberg

Keyword(s):

Saccharomyces Cerevisiae ◽

Nucleotide Sequence ◽

Coding Region ◽

Base Pairs ◽

S1 Nuclease ◽

Calculated Molecular Weight ◽

Base Pair Deletion ◽

S1 Nuclease Mapping ◽

Essential Function ◽

Nuclease Mapping

We determined the complete nucleotide sequence of the RAD3 gene of Saccharomyces cerevisiae. The coding region of the gene contained 2,334 base pairs that could encode a protein with a calculated molecular weight of 89,796. Analysis of RAD3 mRNA by Northern blots and by S1 nuclease mapping indicated that the transcript was approximately 2.5 kilobases and did not contain intervening sequences. Fusions between the RAD3 gene and the lac'Z gene of Escherichia coli were constructed and used to demonstrate that the RAD3 gene was not inducible by DNA damage caused by UV radiation or 4-nitroquinoline-1-oxide. Two UV-sensitive chromosomal mutant alleles of RAD3, rad3-1 and rad3-2, were rescued by gap repair of a centromeric plasmid, and their sequences were determined. The rad3-1 mutation changed a glutamic acid to lysine, and the rad3-2 mutation changed a glycine to arginine. Previous studies have shown that disruption of the RAD3 gene results in loss of an essential function and is associated with inviability of haploid cells. In the present experiments, plasmids carrying the rad3-1 and rad3-2 mutations were introduced into haploid cells containing a disrupted RAD3 gene. These plasmids expressed the essential function of RAD3 but not its DNA repair function. A 74-base-pair deletion at the 3' end of the RAD3 coding region or a fusion of this deletion to the E. coli lac'Z gene did not affect either function of RAD3.

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