Human Jk Recombination Signal Binding Protein Gene (IGKJRB): Comparison with Its Mouse Homologue

Amakawa, Ryuichi; Wu, Jing; Ozawa, Kazuo; Matsunami, Norisada; Hamaguchi, Yasushi; Matsuda, Fumihiko; Kawaichi, Masashi; Honjo, Tasuku

doi:10.1006/geno.1993.1326

Cited by 59 publications

(65 citation statements)

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“…In situ hybridization demonstrated that the pseudogenes, K2 and K7, were localized at chromosomes 9p13 and 9q13, respectively. Their physical maps differed from those of the true functional gene and of the pseudogenes reported previously by Amakawa et al (1993). …”

contrasting

confidence: 83%

“…These are RAG-1 (Mombaerts et al, 1992), RAG-2 (Shinkai et al, 1992), the scid gene (Lieber et al, 1988;Fulop and Philips, 1990) and RBP-Jk. The RBP-Jk gene has been identified in various species, such as Drosophila, mouse, and human (Furukawa et aI., 1991(Furukawa et aI., , 1992Matsunami et al, 1989;Kawaichi et al, 1992;Amakawa et al, 1993), as have analogous pseudogenes (Amakawa et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

“…The RBP-Jk gene has been shown to have been highly conserved during evolution from Drosophila to human (Furukawa et al, 1991;Amakawa et al 1993). The Drosophila RBP-Jk protein is 75~ identical to its murine counterpart (Furukawa et al.…”

Section: Introductionmentioning

confidence: 99%

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Genomic structure and chromosomal localization of processed pseudogenes for human RBP-Jk

Zhang

Tang²,

Jin

et al. 1994

Jap J Human Genet

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SummaryThe functional gene for human recombination signal sequence-binidng protein (RBP-Jk) and corresponding processed psudogenes have been isolated from various species, such as Drosophila, Xenopus, mouse, and human. Here we report the isolation of another two genomic pseudogenes of human RBP-Jk, named K2 and K7, from a cosmid library of Hela cells. The nucleotide sequences of both genes exhibited more than 95 ~ homology to the functional human gene for RBP-Jk. Moreover, they did not contain any intron sequences and were interrupted by several stop codons in all frames. In situ hybridization demonstrated that the pseudogenes, K2 and K7, were localized at chromosomes 9p13 and 9q13, respectively. Their physical maps differed from those of the true functional gene and of the pseudogenes reported previously by Amakawa et al. (1993).

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confidence: 83%

Section: Introductionmentioning

confidence: 99%

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Genomic structure and chromosomal localization of processed pseudogenes for human RBP-Jk

Zhang

Tang²,

Jin

et al. 1994

Jap J Human Genet

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“…This contention is supported by the observation that the 27 C-terminal amino acids of SLIMMER are identical to the RBP-J binding region of KyoT2. KyoT2 complexes via this 27-amino acid domain with, and thereby regulates, RBP-J, a highly conserved DNA-binding protein present in embryonic and all adult tissues (47,48). KyoT2 represses Notch-activated transcription by competing with Notch for binding to RBP-J and by displacing RBP-J from DNA promoter sequences (27).…”

Section: Function Of Nuclear Localization and Export Sequences In Sol8mentioning

confidence: 99%

Characterization of Two Isoforms of the Skeletal Muscle LIM Protein 1, SLIM1

Brown¹,

Mcgrath²,

Ooms³

et al. 1999

Journal of Biological Chemistry

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We have cloned and characterized a novel isoform of the skeletal muscle LIM protein 1 (SLIM1), designated SLIMMER. SLIM1 contains an N-terminal single zinc finger followed by four LIM domains. SLIMMER is identical to SLIM1 over the first three LIM domains but contains a novel C-terminal 96 amino acids with three potential bipartite nuclear localization signals, a putative nuclear export sequence, and 27 amino acids identical to the RBP-J binding region of KyoT2, a murine isoform of SLIM1. SLIM1 localized to the cytosol of Sol8 myoblasts and myotubes. SLIMMER was detected in the nucleus of myoblasts and, following differentiation into myotubes, was exclusively cytosolic. Recombinant green fluorescent protein-SLIM1 localized to the cytoplasm and associated with focal adhesions and actin filaments in COS-7 cells, while green fluorescent protein-SLIMMER was predominantly nuclear. SLIMMER truncation mutants revealed that the first nuclear localization signal mediates nuclear localization. The addition of the proposed nuclear export sequence decreased the level of exclusively nuclear expression and increased cytosolic SLIMMER expression in COS-7 cells. The leucine-rich nuclear export signal was required for the export of SLIMMER from the nucleus of myoblasts to the cytoplasm of myotubes. Collectively, these results suggest distinct roles for SLIM1 and SLIMMER in focal adhesions and nuclear-cytoplasmic communication.The LIM domain is a double zinc finger motif that mediates the protein-protein interactions of transcription factors, signaling, and cytoskeleton-associated proteins (1-4). LIM is an acronym of the three transcription factors, Lin-11, Isl-1, and Mec-3, in which the motif was first identified (5). The LIM domain contains 50 -60 amino acids, with the consensus sequence (CX 2 CX 17-19 HX 2 C)X 2 (CX 2 CX 16 -20 CX 2 (H/D/C)). The conserved cysteine and histidine residues form two zinc-binding pockets stabilizing the tertiary structure of the protein (6, 7). Despite their structural resemblance to GATA-1 zinc fingers, there is no evidence that LIM domains bind DNA directly. Instead, an increasing number of studies implicate LIM domains in protein-protein interactions that regulate development, cellular differentiation, and the cytoskeleton (8, 9).It has been proposed that LIM proteins form a scaffold upon which the coordinated assembly of proteins occurs (8,10). No single LIM domain-binding motif has been identified. LIM domains can associate with other LIM domains to form homoor heterodimers (8, 11). In addition, LIM domains also bind tyrosine-containing motifs, PDZ domains, ankyrin repeats, and helix-loop-helix domains in proteins lacking LIM domains including tyrosine and serine/threonine kinases, cytoskeletal proteins, and transcription factors (12)(13)(14)(15)(16).LIM proteins have been demonstrated in both the nucleus and cytoplasm. LIM homeodomain and LMO proteins are nuclear proteins, which regulate transcription by forming complexes with other transcription factors (2, 10). Members of the cysteine-rich...

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“…Activation of Su(H) is thought to be dependent on a direct physical interaction with the Notch cytoplasmic domain. Homologs of these proteins have been described in Xenopus (Wettstein et al 1997), mouse (Matsunami et al 1989), and humans (Amakawa et al 1993) suggesting a high degree of evolutionary conservation. For example, the mammalian homolog of Su(H), CBF1/RBP-J , can bind and stimulate promoters of the mouse Hairy enhancer of split (HES-1) genes in the presence of vertebrate Notch (Jarriault et al 1995).…”

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confidence: 99%

A histone deacetylase corepressor complex regulates the Notch signal transduction pathway

Kao¹,

Ordentlich²,

et al. 1998

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Human Jk Recombination Signal Binding Protein Gene (IGKJRB): Comparison with Its Mouse Homologue

Cited by 59 publications

References 0 publications

Genomic structure and chromosomal localization of processed pseudogenes for human RBP-Jk

Genomic structure and chromosomal localization of processed pseudogenes for human RBP-Jk

Characterization of Two Isoforms of the Skeletal Muscle LIM Protein 1, SLIM1

A histone deacetylase corepressor complex regulates the Notch signal transduction pathway

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