High impact information on NOLA2

• In vitro reconstitution experiments show that NHP-1 and NHP-2 increase the binding efficiency of the estradiol-receptor complex to the estradiol response element [1].
• Immunofluorescence microscopy experiments showed that hGAR1, hNOP10, and hNHP2 are localized in the dense fibrillar component of the nucleolus and in Cajal (coiled) bodies [2].
• Multiple sequence alignment revealed that SBP2 and the U4 snRNA-binding protein 15.5 kD/Snu13p share the same RNA binding domain of the L7A/L30 family, also found in the box H/ACA snoRNP protein Nhp2p and several ribosomal proteins [3].
• We include new data showing that LNCaP, PC3, and Du145 cells express much lower levels of 5-LOX mRNA and protein compared with normal prostate epithelial cells (NHP2) and primary prostate carcinoma cells (TP1) [4].
• Expression of the human homologue of the small nucleolar RNA-binding protein NHP2 gene during monocytic differentiation of U937 cells [5].

Biological context of NOLA2

• Sequentially, a full-length cDNA of human NHP2 was isolated and the nucleotide sequence was determined [5].
• Removal of TPA restored cell growth through the retrodifferentiation process and subsequent expression of NHP2 [5].
• The expression of NHP2 mRNA during the cell cycle progression of Jurkat T cells also reached a maximum between late G(1) and S phase [5].
• These results indicate that the human NHP2 gene may be regulated at the transcription level depending on tissue specificity and cellular proliferative status, and that the down-regulation of NHP2 expression during induced differentiation of U937 cells may result from the growth arrest accompanying the differentiation [5].
• The NHP2 gene has a predicted 153 amino acid open reading frame, encoding 17.2 kDa protein that shares 38.4% and 44.4% identity with Saccharomyces cerevisiae NHP2 and Schizosaccharomyces pombe nhp2+, respectively [5].

Anatomical context of NOLA2

• NHP2 mRNA, undetectable in human peripheral T cells, was induced at a maximum level between late G(1) and S phase after polyclonal activation [5].
• In healthy human tissues, NHP2 mRNA was expressed at high levels in spleen, thymus, prostate, testis, ovary, small intestine, colon (mucosal lining), heart, brain, placenta, skeletal muscle, kidney and pancreas, and at low levels in liver, and very weakly in peripheral blood leukocyte and lung [5].
• The human homologue of yeast NHP2, which is known to be a core protein component of yeast H/ACA small nucleolar ribonucleoprotein particles (snoRNPs), was identified by ODD-PCR as a 313-bp cDNA fragment exhibiting a distinct decrease in its expression level during TPA-induced differentiation of promonocytic U937 into monocytes and macrophages [5].

References