Disease relevance of HN1L

• Although L11 is the most highly methylated protein in the E. coli ribosome, the sites of methylation are not conserved in the archaebacterial L11e proteins [1].
• Isolation by gel filtration and ion-exchange chromatography of a carbohydrate-rich LPS from phenol-water extracts of leptotrichia buccalis strain L11 [2].

High impact information on HN1L

• This direct interaction with a key ribosomal RNA tertiary interaction suggests that part of the role of L11 is to stabilize an unusual RNA fold within the ribosome [3].
• The presence of a unique flexible loop in the cofactor-binding site suggests how exchange of AdoMet with the reaction product S-adenosyl-L-homocysteine can occur without necessitating the dissociation of PrmA from L11 [4].
• Two apo-PrmA structures at 1.59 and 2.3 A resolution and a third with bound cofactor S-adenosyl-L-methionine at 1.75 A each exhibit distinct relative positions of the substrate recognition and catalytic domains, revealing how PrmA can position the L11 substrate for multiple, consecutive side-chain methylation reactions [4].
• Here, we show that cancer-associated missense mutations targeting MDM2's central zinc finger disrupt the interaction of MDM2 with L5 and L11 [5].
• A unique mAb to murine CD43, L11, has recently been shown to block the migration of T cells from blood into organized lymphoid tissues [6].

Chemical compound and disease context of HN1L

• Experiments using these assays with both an Escherichia coli rRNA fragment and a thermostable variant of that RNA show that Mg(2+), L11 and thiostrepton all induce the RNA to fold to an essentially identical tertiary structure [7].

Biological context of HN1L

• HN1 is mapped on chromosome 17q25.2, with two transcripts (1.0 and 1.6 kb in length, respectively) due to alternative splicing [8].
• Based on sequence alignments and phylogenetic analysis, all these homologous genes and pseudogenes were defined as a HN1 gene family [8].
• Additionally, we identified nine pseudogenes of HN1 (six) and HN1L (three) in the genomes of the human, mouse and rat [8].
• The present work reported the cloning and characterization of two novel human genes--HN1 (hematopoietic- and neurologic-expressed sequence 1) and HN1L (HN1-like gene) which are proposed to be involved in embryo development [8].
• The binding site of thiostrepton on L11 was also defined by analysis of structural and dynamics data and chemical shift mapping [9].

Anatomical context of HN1L

• HN1 is expressed abundantly in testis and skeletal muscle among 16 human tissues, and it is localized in the nucleus indicated by GFP fusion expression [8].
• The sequence of KIF3C predicts an unusually long insertion in the proximity of L11, a region thought to mediate microtubule binding [10].

Associations of HN1L with chemical compounds

• Animals representing all of these groups were injected (between L11 and L11.75) with either vehicle, or a low dose (25 micrograms) or a high dose (2,500 micrograms) of melatonin daily for 28 days, after which they were killed, and the adrenals were collected for assay of DBH activity by means of a sensitive radioenzymatic method [11].
• Responses of P1 were negatively affected by individual aa replacement by alanine at eight aa positions within the 17mer peptide (F4, K5, Q6, K9, L11, Q12, R13, P14) [12].
• Axially chiral thioamide ligands L5, L6, L8, L11, and bis(thioamide) ligand L13 were prepared from the reaction of (S)-(-)-1,1'-binaphthyl-2,2'-diamine with acyl chlorides and phosphorus pentasulfide (P2S5) [13].
• In addition LPS from L11 contained 2-keto-3-deoxyoctonate and an unidentified aldose [14].
• Scintillation proximity assays designed to look at the binding of the L11 C-terminal RNA-binding domain to a 23S ribosomal RNA (rRNA) fragment, as well as the ability of thiostrepton to induce that binding, were used to demonstrate the role of Mg(2+), L11 and thio-strepton in the formation and maintenance of the rRNA fragment tertiary structure [7].

Analytical, diagnostic and therapeutic context of HN1L

• Western blot confirmed that HN1 encodes a 16.5-kDa protein [8].
• Serotype L10 and L11 group A meningococal LOS were chemically modified and used to investigate what portion of the LOS molecule is important for expression of the conserved (D6A) epitope and serotype-associated LOS epitopes by use of immunoblotting techniques and selected MAbs as probes [15].
• The 16 hamsters were distributed between three injections groups: vehicle only, 25 micrograms and 2500 micrograms melatonin (M) by subcutaneous injection daily at L11 to L11.75 in a LD 14:10 daily photoperiod [16].

References