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Digitale Medien

Multiple tandemly repeated binding sites for the YY1 repressor and transcription factors AP-1 and SP-1 are clustered within intron-1 of the gene encoding the IE110 transactivator of herpes simplex virus Type 1 (1995)

Gu, Wei ; Huang, Qi ; Hayward, Gary S.

Springer

Journal of biomedical science 2 (1995), S. 203-226

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ISSN: 1423-0127

Schlagwort(e): Transcription factor binding sites ; DNaseI footprinting ; TPA response elements ; Type-specific control region

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie , Medizin

Notizen: Abstract Expression of the IE110 (ICP0) transactivator protein of HSV appears to be critical for reactivation from the latent state and occurs at immediate-early times during the lytic cycle under the control of an upstream divergent enhancer-promoter region that contains multiple Oct and Sp-1 binding sites overlapping with VP16 response elements. Surprisingly, the large 800-bp first intron of the HSV-1 IE110 gene also proved to have a complex repetitive organization encompassing multiple transcription factor binding sites within four distinct domains. DNase I footprinting studies revealed that 13 of 17 copies of a 15-bp repeated element represented high-affinity binding sites for the cellular YY1 repressor protein. Between 4 and 7 of these sites are direct tandem repeats and the rest are interspersed with three repeated AT-rich motifs and a dyad symmetry region containing two strong AP-1 binding sites and an adjacent SP-1 binding site on each arm. Several of the YY1 sites also bound weakly to SRF. The intron also contains four clustered purine/pyrimidine tracts of between 16 and 23 bp long. Both the AP-1/AP-2/SP-1 dyad protein binding region and, to a lesser extent, the YY1 tandem-repeat cluster conferred responsiveness to TPA when placed upstream of a heterologous promoter in transient expression assays. The functional significance of the HSV-1 IE110 intron region is unknown as yet, but the novel arrangement of tandemly repeated YY1 sites has the potential to produce structural bending and transcriptional attenuation effects. Interestingly, few of these transcription factor binding motifs are conserved in the equivalent IE110 intron of HSV-2, and the domain appears to represent a unique alternative control region that is specific for HSV-1.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF02253381

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Digitale Medien

Poly (A) binding protein is bound to both stored and polysomal mRNAs in the mammalian testis (1995)

Gu, Wei ; Kwon, Yunhee ; Oko, Richard ; [weitere]

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

Molecular Reproduction and Development 40 (1995), S. 273-285

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ISSN: 1040-452X

Schlagwort(e): Spermatogenesis ; RNA-binding proteins ; Testis ; Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie

Notizen: RNA-binding proteins that bind to the 3′ untranslated region of mRNAs play important roles in regulating gene expression. Here we examine the association between the 70 kDa poly (A) binding protein (PABP) and stored (RNP) and polysomal mRNAs during mammalian male germ cell development. PABP mRNA levels increase as germ cells enter meiosis, reaching a maximum in the early postmeiotic stages, and decreasing to a nearly nondetectable level towards the end of spermatogenesis. Most of the PABP mRNA is found in the nonpolysomal fractions of postmitochondrial extracts, suggesting that PABP mRNA is either inefficiently translated or stored as RNPs during spermatogenesis. Virtually all of the testicular PABP is bound to either polysomal or nonpolysomal mRNAs, with little, if any, free PABP detectable. Analysis of several specific mRNAs reveals PABP is bound to both stored (RNP) and translated forms of the mRNAs. Western blot analysis and immunocytochemistry indicate PABP is widespread in the mammalian testis, with maximal amounts detected in postmeiotic round spermatids. The presence of PABP in elongating spermatids, a cell type in which PABP mRNA is nearly absent, suggests that PABP is a stable protein in the later stages of male germ cell development. The high level of testicular PABP in round spermatids and in mRNPs suggests a role for PABP in the storage as well as in the subsequent translation of developmentally regulated mRNAs in the mammalian testis. © 1995 Wiley-Liss, Inc.

Zusätzliches Material: 9 Ill.