High impact information on NAT14

• Computational analysis revealed that Klp1 has a leucine-zipper-like structure, a Leu-X-X-Leu-Leu motif, and a putative nuclear localization signal in the basic amino acid rich region [1].
• Klp1 mRNA was highly expressed in K562 cells, HeLa cells, and brain as a single transcript (1.4 kb) [1].
• Transfection of the Klp1 expression vector into THP-1 cells resulted in transcriptional activation of a reporter construct containing CPRE [1].
• These results indicate that Klp1 is a DNA sequence-specific transcription factor that regulates gene expression of genes that contain CPRE in their regulatory region [1].
• To isolate a CPRE binding protein, we performed Southwestern screening of K562 cDNA expression library using CPRE as a probe and isolated a cDNA clone which encoded a novel protein, Klp1 (K562 cell-derived leucine-zipper-like protein 1) [1].

Biological context of NAT14

• These structural characteristics and the promoter function suggest that Klp1 may play a role in cell cycle regulation [2].
• In order to clarify the function of Klp1, we determined the complete human Klp1 genomic structure and regulatory element in the promoter region [2].

Other interactions of NAT14

• PF16, PF20 and KLP1 have been sequenced and their gene products localized [3].

Analytical, diagnostic and therapeutic context of NAT14

• Gel mobility shift assays revealed that Klp1 specifically binds to CPRE [1].
• We have performed immunological tests on isolated sunfish rod inner-outer segments (RIS-ROS) using two antibodies that recognize the conserved motor domain of numerous KIFs (anti-LAGSE, a peptide antibody, and anti-Klp1 head, generated against the N terminus of Chlamydomonas Klp1) as well as an antibody specific to a neuronal KIF, KIF3A [4].

References