mu-crystallin is a mammalian homologue of Agrobacterium ornithine cyclodeaminase and is expressed in human retina.

Kim, Robert Y.; Gasser, Robin B.; Wistow, Graeme

doi:10.1073/pnas.89.19.9292

Cited by 75 publications

(68 citation statements)

References 19 publications

(33 reference statements)

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“…CRYM, a taxon-specific 35-kDa protein, is a major structural kangaroo lens protein and is also highly expressed in brain, muscle, and kidney (Wistow and Kim 1991;Kim et al 1992). Southern blot analysis indicated that a single gene for human CRYM is located on Chromosome 16p (Chen et al 1992).…”

mentioning

confidence: 99%

Crystal structure of human μ‐crystallin complexed with NADPH

Cheng

Sun

et al. 2007

Protein Science

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Human cytosolic 3,5,39-triiodo-L-thyronine-binding protein, also called m-crystallin or CRYM, plays important physiological roles in transporting 3,5,39-triiodo-L-thyronine (T 3 ) into nuclei and regulating thyroid-hormone-related gene expression. The crystal structure of human CRYM's bacterial homolog Pseudomonas putida ornithine cyclodeaminase and Archaeoglobus fulgidus alanine dehydrogenase have been available, but no CRYM structure has been reported. Here, we report the crystal structure of human CRYM bound with NADPH refined to 2.6 Å , and there is one dimer in the asymmetric unit. The structure contains two domains: a Rossmann fold-like NADPH-binding domain and a dimerization domain. Different conformations of the loop Arg83-His92 have been observed in two monomers of human CRYM in the same asymmetric unit. The peptide bond of Val89-Pro90 is a trans-configuration in one monomer but a cis-configuration in the other. A detailed comparison of the human m-crystallin structure with its structurally characterized homologs including the overall comparison and superposition of active sites was conducted. Finally, a putative T 3 -binding site in human CRYM is proposed based on comparison with structural homologs.

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confidence: 99%

Crystal structure of human μ‐crystallin complexed with NADPH

Cheng

Sun

et al. 2007

Protein Science

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“…Northern blotting in eight human tissues demonstrated that p38CTBP is a single mRNA species (23). As shown in the Results, dot hybridization demonstrated that there is heterogeneous expression of p38CTBP in the central nervous system.…”

Section: Discussionmentioning

confidence: 78%

“…The m-crystallin protein, a taxon-specific 35 kDa protein that is highly expressed in lens (22), brain, muscle and kidney in the kangaroo (23), may be important in maintaining structural function in these tissues of the kangaroo. Kim et al (23) also reported the cloning of m-crystallin cDNA from human retina and showed that it was expressed at high levels in human neural tissue, muscle and kidney.…”

Section: Introductionmentioning

confidence: 99%

Cell-specific expression of NADPH-dependent cytosolic 3,5,3'-triiodo-L-thyronine-binding protein (p38CTBP)

Suzuki

Mori²,

Kobayashi³

et al. 2003

European Journal of Endocrinology

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We have previously shown that cytosolic 3,5,30 -triiodo-L-thyronine (T3)-binding protein (CTBP) possesses a high affinity for T3 binding in the presence of nicotinamide adenine dinucleotide phosphate in vitro, and that p38CTBP increases intracellular content of T3, and suppresses T3-mediated transactivity. Screening of mRNA expression in 73 different human tissues has demonstrated that p38CTBP mRNA is expressed at high levels in brain and heart. We have examined the intracellular localization and tissue-specific distribution of this protein by using a specific antibody against human p38CTBP. Western blotting and immunoprecipitation studies have shown that the antibody recognizes human p38CTBP. Interaction of p38CTBP with the antibody did not affect the T3-binding activity of p38CTBP, and its dimer formation in vitro. Western blotting analysis has shown that p38CTBP is expressed in brain and heart predominantly, similar to the distribution of mRNA. Immunohistochemical studies have demonstrated p38CTBP in neural cells and cardiac muscle cells. p38CTBP localizes in cytoplasm rather than in nuclei in neural cells. The evidence for the presence of tissue-specific localization of p38CTBP has indicated that p38CTBP has a tissue-specific function, such as the regulation of T3 delivery from cytoplasm to nuclei.

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“…This ORF has a length of 1113 nt and shows weak similarity to the mammalian homologue of Agrobacterium ornithine cyclodeaminase (Kim et al, 1992). However, loss of this ORF had no influence on the phenotype of the yeast cell under the conditions tested.…”

Section: Ygl159wmentioning

confidence: 97%

Basic functional analysis of six unknown open reading frames from Saccharomyces cerevisiae: four from chromosome VII and two from chromosome XV

Pearson¹,

Schweizer²

2001

Yeast

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Six open reading frames (ORFs) of unknown function from Saccharomyces cerevisiae from the left arms of chromosomes VII and XV were disrupted by the short-flanking homology method in the diploid strains FY1679 and CENPK2. In each case, the entire ORF, with the exception of the first nucleotide of the start codon, was eliminated and replaced by the kanMX4 cassette. Correct integration of the disrupting marker was checked by colony PCR of the geneticin (G418)-resistant transformants. Sporulation followed by tetrad dissection of the diploids revealed that none of the ORFs encoded a product essential for the viability of either yeast strain. The neutral effect of these disruptions extended to mating and sporulation, since it was possible to create homozygous diploid disruptants that were capable of sporulation. Basic phenotypic analysis was carried out on all strains by growing them on three different media at three different temperatures and revealed no significant differences between disruptants and the parental strains. A cognate clone and a kanMX4 disruption cassette were created for five of the six ORFs by gap repair with specific long-flanking homology cassettes. For experimental reasons, the cognate clone and disruption cassette corresponding to the sixth ORF (YGL161w) had to be created by PCR.

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mu-crystallin is a mammalian homologue of Agrobacterium ornithine cyclodeaminase and is expressed in human retina.

Cited by 75 publications

References 19 publications

Crystal structure of human μ‐crystallin complexed with NADPH

Crystal structure of human μ‐crystallin complexed with NADPH

Cell-specific expression of NADPH-dependent cytosolic 3,5,3'-triiodo-L-thyronine-binding protein (p38CTBP)

Basic functional analysis of six unknown open reading frames from Saccharomyces cerevisiae: four from chromosome VII and two from chromosome XV

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