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PubMed2003

Mussel MAP, a major gonad-duct esterase-like protein, is released into sea water as a dual constituent of the seminal fluid and the spermatozoon.

Our interest in the comparative analysis of male reproductive-tract esterases in different animal groups has led us to undertake a detailed study of the Mytilus galloprovincialis male-associated polypeptide (MAP) throughout the mussel gonad-duct tract and at spawning. The results of this work indicate that MAP is a major protein in M. galloprovincialis semen, with dual presence in both sperm cells and cell-free seminal fluid. Shortly after spawning, the released sperm mass is subdivided in diffused cloudy-like and thread-shaped 'clots', in which a soluble-phase MAP may persist as long as the clots keep their compact form. Additional experiments involving the incubation of spawned spermatozoa at increasing Triton X-100 concentrations demonstrated that MAP is also strongly associated with sperm cells. These results were further validated by immunofluorescent staining, which revealed that MAP is localized in the mid-piece region of spawned spermatozoa. This unexpected finding raises the possibility that MAP may play a role in sperm fertility in bivalves. Using whole-mount histology and micromanipulation techniques, we studied the structural patterning of the mantle gonad-duct network and assessed the sampling of luminal contents from the ducts. Of particular interest is the observation that MAP content in the luminal fluid increases from the lumen of the spermatogenic tubules to that of the collecting gonad ducts, where MAP is detected at a very high concentration. These high levels may lead to a significant presence of MAP in semen and consequently to a prolonged survival of sperm spawned at sea. In addition, data related to the potential structural similarity between mussel MAP and esterase S of the Drosophila virilis ejaculatory bulb are presented and discussed. Finally, we show that the 64kDa protein of human semen reveals positive cross-reactivity with antibodies directed against Mytilus MAP and Drosophila esterase S. Taken together, the results reveal mussel MAP as the only esterase-like protein described so far whose distribution in the gonad and semen can be specifically associated with maturation, transport, emission and survival of spermatozoa outside.

Amino Acid Sequence↗
PubMed2003

Mean arterial pressure and pulse pressure are associated with different clinical parameters in chronic haemodialysis patients.

The mean arterial pressure (MAP) usually serves as an expression of blood pressure in patients on chronic haemodialysis (PCHD), instead of using solely systolic or diastolic pressure. Pulse pressure (PP) has been recognized as an important correlate of mortality in PCHD. We conducted this study in order to demonstrate clinical and biochemical determinants and variability of predialysis and postdialysis MAP and PP values. A total of 136 single haemodialysis (HD) treatments in 23 subjects (PCHD, 11 male and 12 female patients) were processed during 15 months. MAP before HD was in negative correlation with haemoglobin (P<0.001) and body mass index (BMI) (P<0.001), and in positive correlation with weekly erythropoietin dosage (P=0.017). MAP after HD was in negative correlation with haemoglobin (P<0.001), ultrafiltration per HD (P=0.015), and BMI (P=0.001), and in positive correlation with weekly erythropoietin dosage (P=0.003). PP before HD was in negative correlation with parathyroid hormone (PTH) level (P=0.020), haemoglobin (P<0.001), ultrafiltration per HD (P=0.001), and years on the chronic HD treatment (P=0.001), and in positive correlation with weekly erythropoietin dosage (P<0.001) and age (P<0.001). PP after HD was in significant negative correlation with PTH (P=0.015), haemoglobin (P=0.005), ultrafiltration per HD (P<0.001), BMI (P=0.003), and in positive correlation with weekly erythropoietin dosage (P<0.001) and age (P=0.004). Multiple regression analyses unveiled the strongest and negative correlations between MAP before HD and BMI (beta=-0.37, P=0.01); MAP after HD and haemoglobin (beta=-0.36, P=0.01); PP after HD and ultrafiltration/body weight ratio (beta=-0.41, P<0.001). The strongest and positive correlation was found between PP before HD and erythropoietin dosage per week (beta=0.51, P&<0.001). In conclusion, our findings support the assumption that PP and MAP are associated with different clinical parameters. PP values have advantages as the method of blood pressure expression.

Alkaline Phosphatase↗
PubMed1983

Extensive cAMP-dependent and cAMP-independent phosphorylation of microtubule-associated protein 2.

Microtubule-associated protein 2 (MAP 2) is the major substrate for phosphorylation in purified preparations of brain microtubules. In earlier work, we showed that phosphorylation is catalyzed by a type II cAMP-dependent protein kinase tightly associated with MAP 2 itself. In the present study, we have examined the extent of MAP 2 phosphorylation by its associated protein kinase. Using an inorganic phosphate assay, we found that MAP 2 contained from 8 to 13 mol of phosphate/mol of protein as isolated. The catalytic subunit of the MAP 2-associated kinase catalyzed the incorporation of additional phosphate to a final level of 20-22 mol/mol of MAP 2. Potato acid phosphatase was used to remove phosphate from MAP 2. Rephosphorylation of acid phosphatase-treated MAP 2 resulted in maximal incorporation of 13 mol of phosphate/mol of MAP 2. The rates and extent of [32P] phosphate incorporation into as isolated and dephosphorylated MAP 2 were found to be identical, and phosphate was incorporated into identical peptides in the two preparations. These results were interpreted to indicate that MAP 2 contains as many as 13 cAMP-dependent phosphorylation sites, and approximately eight phosphates of as yet undetermined origin.

Animals↗
PubMed1995

Enhanced interaction between tubulin and microtubule-associated protein 2 via inhibition of MAP kinase and CDC2 kinase by paclitaxel.

Paclitaxel, an anti-mitotic anti-cancer agent, is active against solid tumors. The inhibition of depolymerization and promotion of microtubular assembly are essential for the anti-tumor activity of paclitaxel. Microtubule-associated proteins (MAPs) co-polymerize with tubulin and play some roles in microtubular dynamics. We examined the effect of paclitaxel on the interaction between tubulin and MAPs. Human lung-cancer cells, PC-14, were synchronized to G1/S border by the thymidine-double-block technique. After release from exposure to thymidine, the cells were treated briefly with 2 nM paclitaxel and the levels of alpha and beta tubulins and MAPs were examined after various times. Immunoblot analysis of paclitaxel-treated cells showed no changes in the overall expression of alpha and beta tubulins, microtubule-associated protein 2 (MAP2) or MAPs in comparison with controls. The samples were immunoprecipitated with anti-alpha- and anti-beta-tubulin antibodies and reblotted with an anti-MAP2 antibody, which showed that the amount of co-immuno-precipitated MAP2 in the synchronized cells, were increased by the brief paclitaxel treatment. These results suggest that paclitaxel treatment enhances the interaction between alpha and beta tubulins and MAP2. Since the phosphorylation state of MAP2 regulates the affinity of MAP2 for tubulins, and mitogen-activated protein (MAP) kinase is considered to be one of the kinases responsible for MAP2 phosphorylation, the effect of paclitaxel treatment on the MAP-kinase activity of synchronized PC-14 cells was examined. Two bands with molecular masses of 42 and 44 kDa were detected by an "intra-gel" MAP-kinase assay using myelin basic protein as the substrate. Paclitaxel treatment inhibited the MAP-kinase activity of PC-14 cells and inhibition was maximal at the G2/M phase of the cell cycle. Similar, concentration-dependent inhibition by paclitaxel of cellular MAP kinase of human synchronized small-cell lung carcinoma, H69, was observed. No inhibition of the MAP kinase of the paclitaxel-resistant sub-line H69/Txl by paclitaxel was observed, suggesting that some change of the MAP-kinase cascade had occurred in these cells. No direct inhibition of MAP-kinase activity by paclitaxel was observed in the cell-free assay (in vitro), suggesting that paclitaxel did not inhibit MAP kinase directly. Since it has been speculated that p34cdc2 kinase is also a kinase that phosphorylates MAP2, the effect of paclitaxel treatment on the p34cdc2-kinase activity of synchronized PC-14 and PC-9 cells was examined. Paclitaxel inhibited p34cdc2-kinase activation at the G2/M phase. These results suggest that paclitaxel inhibited MAP kinase and p34cdc2 kinase in vivo indirectly. These actions of paclitaxel may be responsible for the increased affinity between MAP2 and tubulins that it induces.

Amino Acid Sequence↗
PubMed1992

Related subunits of NF-kappa B map to two distinct loci associated with translocations in leukemia, NFKB1 and NFKB2.

The chromosomal locations of the human genes NFKB1 and NFKB2, which encode two alternative DNA binding subunits of the NF-kappa B complex, p105 and p49/p100, respectively, have been determined. p105 was assigned to 4q21.1-q24 and p49/p100 to chromosome 10 by Southern blot analysis of panels of human/Chinese hamster cell hybrids. The locations were confirmed by fluorescence in situ hybridization and mapped with greater resolution to 4q23 and 10q24, respectively. These results demonstrate that these members of the NF-kappa B family are unlinked. Interestingly, p49/p100 as well as p105 maps to regions associated with certain types of acute lymphoblastic leukemia.

Animals↗
PubMed1999

Spontaneous recurrence of methampetamine psychosis: increased sensitivity to stress associated with noradrenergic hyperactivity and dopaminergic change.

We studied the factors precipitating spontaneous recurrences of methamphetamine (MAP)-induced paranoid-hallucinatory states (referred to as "flashbacks") in 28 flashbackers, along with 18 non-flashbackers with a history of MAP psychosis. Plasma levels of catecholamines and their metabolites were assayed in the 28 flashbackers, the 18 non-flashbackers, 8 subjects with persistent MAP psychosis, and 33 normal controls (22 MAP users and 11 non-users). The flashbackers had been exposed to significantly higher numbers of stressful events, and/or MAP-induced frightening paranoid-hallucinatory states during previous MAP use, than the non-flashbackers. Factors triggering the flashbacks met the DSM-III-R criteria for a mild psychosocial stressor. During flashbacks, plasma norepinephrine levels increased and plasma levels of 3-methoxytyramine, which is an indicator of dopamine release, showed a smaller increase. It follows that stressful experiences together with MAP use may induce sensitization to mild psychosocial stressors. Noradrenergic hyperactivity and some degree of increased dopamine release may be involved in this process. Stress sensitization may elicit memories of MAP psychosis associated with stressful experiences in response to mild psychosocial stressors, leading to the occurrence of flashbacks. Sensitization to stress associated with noradrenergic hyperactivity, involving increased dopamine release may be central to spontaneous recurrences of MAP psychosis.

Adaptation, Psychological↗
PubMed2000

The Xenopus XMAP215 and its human homologue TOG proteins interact with cyclin B1 to target p34cdc2 to microtubules during mitosis.

Cytoskeleton reorganization, leading to mitotic spindle formation, is an M-phase-specific event and is controlled by maturation promoting factor (MPF: p34cdc2-cyclinB1 complex). It has previously been demonstrated that the p34cdc2-cyclin B complex associates with mitotic spindle microtubules and that microtubule-associated proteins (MAPs), in particular MAP4, might be responsible for this interaction. In this study, we report that another ubiquitous MAP, TOG in human and its homologue in Xenopus XMAP215, associates also with p34cdc2 kinase and directs it to the microtubule cytoskeleton. Costaining of Xenopus cells with anti-TOGp and anti-cyclin B1 antibodies demonstrated colocalization in interphase cells and also with microtubules throughout the cell cycle. Cyclin B1, TOG/XMAP215, and p34cdc2 proteins were recovered in microtubule pellets isolated from Xenopus egg extracts and were eluted with the same ionic strength. Cosedimentation of cyclin B1 with in vitro polymerized microtubules was detected only in the presence of purified TOG protein. Using a recombinant C-terminal TOG fragment containing a Pro-rich region, we showed that this domain is sufficient to mediate cosedimentation of cyclin B1 with microtubules. Finally, we demonstrated interaction between TOG/XMAP215 and cyclin B1 by co-immunoprecipitation assays. As XMAP215 was shown to be the only identified assembly promoting MAP which increases the rapid turnover of microtubules, the TOG/XMAP215-cyclin B1 interaction may be important for regulation of microtubule dynamics at mitosis.

Animals↗
PubMed1998

Effects of diabetes and difluoromethylornithine treatment on hyperplasia, activity of MAP-kinase, and activity and association with cyclin B of p34cdc2 kinase in rat jejunal mucosa.

BACKGROUND: The different signal transduction pathways of rapidly proliferating cells of the intestine are not clearly understood. We report here a possible signaling pathway that involves regulation of activity of two closely related kinases, MAP-K (mitogen-activated protein kinase) and p34cdc2 kinase, during hyperplasia of diabetic jejunal mucosa. Our aim was to investigate the activity and phosphorylation of MAP-K and activity and association of p34cdc2 kinase with cyclin B during diabetes-induced jejunal mucosal hyperplasia in vivo. METHODS: We studied untreated and difluoromethylornithine (DFMO) treated control rats and rats with streptozotocin-induced type I diabetes. Assays were done 10 days after the induction of diabetes. In diabetic rats there was jejunal hyperplasia as indicated by increases in the jejunal mucosal weight/cm and DNA content as well as increased activities of MAP-K and p34cdc2 kinase and association of the latter with cyclin B as compared to corresponding values in control rats. Administration of DFMO, an irreversible inhibitor of the proliferation-associated enzyme ornithine decarboxylase (ODC), prevented diabetes-I induced jejunal hyperplasia and decreased all of the above enzymic parameters in both diabetic and control rats. In our previous in vivo study, DFMO administration also blocked diabetic jejunal hyperplasia and in addition decreased ornithine decarboxylase and tyrosine kinase activities jejunal and tyrosine phosphorylation of proteins. CONCLUSION: Thus the jejunal mucosal hyperplasia found in diabetes appears to involve activation of signal transduction pathways involving tyrosine kinases, MAP-K, p34cdc2 kinase, and cyclin B.

Animals↗
PubMed2003

[Primary analysis on protein maps of Helicobacter pylori strains associated with gastric carcinoma].

OBJECTIVE: To identify specific proteins of Helicobacter pylori (H. pylori) that associated with gastric carcinoma. METHODS: The whole-cell proteins of H. pylori were separated by two-dimensional electrophoresis (2-DE). The protein maps of four H. pylori strains associated with gastric carcinoma and nine strains that isolated from patients with non-gastric carcinoma were then compared by ImageMaster 2D v3.1. MALDI-TOF mass spectrometry was performed to identify the proteins of interest. The proteins were searched by software mascot and identified by peptide fingerprint map. RESULTS: Three proteins seemed to be associated with gastric carcinoma including acylneuraminate cytidylyltransferase with Mowse score 79 with the sequence coverage of 32%. The other two had no unambiguous protein to match. CONCLUSION: Acylneuraminate cytidylyltransferase seemed to be a specific H. pylori protein associated with the presence of gastric carcinoma. Other two were novel proteins that might be associated with gastric carcinoma. However, the mechanism needs to be explored.

Amino Acid Sequence↗
PubMed2006

Overexpression of cyclin D1 is associated with elevated levels of MAP kinases, Akt and Pak1 during diethylnitrosamine-induced progressive liver carcinogenesis.

Hepatocellular carcinoma (HCC) is a multi-factorial and multi-step process. However, the molecular mechanisms, which play a pivotal role during progressive development of HCC, are not known. Accordingly Sprague-Dawley rats were administered diethylnitrosamine (DEN) for one to three months in order to understand the molecular alterations during progressive development of liver tumor. In this study involvement of G1/S regulatory proteins, MAP kinases and cell survival factors were analyzed using RT-PCR, western blotting and in vitro kinase assays. The data showed overexpression of cyclin D1 and increased expression and activation of ERK1/2, p38 kinase and JNK1/2 with progression of tumor suggesting that MAP kinases play an important role during tumorigenesis. These molecular alterations were supported by Akt upregulation and increase in the levels of inactive GSK3beta with progression of liver tumor. Further, p21-actived kinase1 (Pak1) was found to be upregulated with tumor progression, which is a novel observation during progressive liver carcinogenesis. These results indicate that elevated levels of all the three MAP kinases (ERK1/2, p38 and JNK1/2), Akt/GSK3beta and Pak1 are associated with cyclin D1 upregulation, which helps in the disruption of the G1/S regulatory point of the cell cycle and leads to abnormal cell proliferation during progressive hepatocarcinogenesis.

Animals↗
PubMed2001

Myosin VIIA is specifically associated with calmodulin and microtubule-associated protein-2B (MAP-2B).

Myosin VIIA is a motor molecule with a conserved head domain and tail region unique to myosin VIIA, which probably defines its unique function in vivo. In an attempt to further characterize myosin VIIA function we set out to identify molecule(s) that specifically associate with it. We demonstrate that 17 and 55 kDa proteins from mouse kidney and cochlea co-purify with myosin VIIA on affinity columns carrying immobilized anti-myosin VIIA antibody. N-terminal sequencing and immunoblotting analysis identified the 17 kDa protein as calmodulin, whereas MS and immunoblotting analysis identified the 55 kDa protein as microtubule-associated protein-2B (MAP-2B). Myosin VIIA can also be co-immunoprecipitated from kidney homogenate using anti-calmodulin or anti-MAP2 (recognizing isoforms 2A and 2B) antibodies, confirming the strong association between calmodulin and myosin VIIA and between MAP-2B and myosin VIIA. Myosin VIIA binds to calmodulin with an apparent K(d) of 10(-9) M. Scatchard analysis of the binding of myosin VIIA to MAP-2B provided evidence for two binding sites, with K(d) values of 10(-10) and 10(-9) M, which have been mapped to medial and C-terminal tail domains of myosin VIIA. The characterization of the interaction of calmodulin and MAP-2B with myosin VIIA provides new insights into the function of myosin VIIA.

Amino Acid Sequence↗
PubMed1990

Microtubule-associated protein 1A is the fibroblast HMW MAP undergoing mitogen-stimulated serine phosphorylation.

A variety of antibodies to microtubule-associated protein (MAP) have been used to demonstrate that phosphorylation of a 350 kDa microtubule-associated protein is stimulated 2-3 fold by epidermal growth factor or serum in quiescent 3T3-L1 fibroblasts and by insulin in 3T3-L1 adipocytes. Phosphorylation occurs on serine residues, and is maximal by 15-20 min. The phosphoprotein has been identified as MAP1A by specific immunoprecipitation with a well-characterized monoclonal antibody.

Animals↗
PubMed1986

Polyamine regulation of the microtubule-associated protein kinase.

Microtubule protein prepared by cycles of assembly-disassembly contains a cyclic AMP-dependent protein kinase that phosphorylates the high-molecular-weight microtubule-associated protein MAP-2. The polyamine spermine at 2mM affected the phosphorylation of MAP-2 in a manner that depended on the cyclic AMP concentration. At cyclic AMP concentrations below 10(-6) M, spermine increased the rate of phosphorylation, while at cyclic AMP concentrations above 10(-6) M, spermine decreased the rate of phosphorylation. Spermine also decreased the final extent of cyclic AMP-dependent phosphorylation but did not affect the protein substrate specificity of the microtubule-associated protein kinase. MAP-2 was the principal substrate both in the presence and in the absence of spermine. Because of these results, we propose that microtubule protein phosphorylation may be regulated in vivo by spermine as well as by cyclic AMP levels.

Animals↗
PubMed1979

Regulation of the microtubule steady state in vitro by ATP.

ATP increases microtubule steady state assembly and disassembly rates in vitro in a concentration-dependent manner. Bovine brain microtubules, composed of 75% tubulin and 25% high molecular weight microtubule-associated proteins (MAPs), were purified by three cycles of assembly and disassembly in the absence of ATP. When assembled to steady state, these microtubules add dimers at one end and lose them at the other in a unidirectional assembly-disassembly process. In the presence of 1.0 mM ATP the unidirectional flow of tubulin from one end of the microtubules to the other increases as much as 20 fold, as revealed by loss of 3H-GTP from uniformly labeled microtubules under GTP chase conditions and by the rate of disassembly following addition of 50 microM podophyllotoxin. UTP, CTP and 5' adenylylimidodiphosphate (AMP-PNP) cannot substitute for ATP in producing this effect. Furthermore, the increase in steady state flow rate persists afer ATP is removed. Thus microtubules assembled in ATP and centrifuged through sucrose cushions to separate them from nucleotides continue to exhibit increased rates in the next assembly cycle in the absence of ATP. It is possible that an ATP-dependent microtubule protein kinase is responsible for the observed increase in tubulin flow rate. A kinase activity associated with brain MAPs has been reported to be cAMP-dependent (Sloboda et al., 1975). We have found an adenylate cyclase activity associated with these microtubules. Whether the adenylate cyclase is a contaminant or due to a specific microtubules-associated protein, and whether its activity is functionally linked to the increased rate of assembly and disassembly in the presence of ATP, remain to be determined.

Adenosine Triphosphate↗
PubMed1985

Microtubules and nucleoside diphosphate kinase. Nucleoside diphosphate kinase binds to co-purifying contaminants rather than to microtubule proteins.

Nucleoside diphosphate (NDP) kinase has been postulated to generate GTP from the GDP bound to tubulin. The purified chick brain enzyme was studied with respect to its kinetic parameters, and the protein-protein interactions between the NDP kinase and tubulin were examined. No specific interaction is observed between the enzyme and assembled microtubules, tubulin dimers, or tubulin-microtubule-associated protein (MAP) oligomers under a variety of nucleotide conditions. The apparent association is demonstrated to result from NDP kinase binding to a co-purifying contaminant. The absence of detectable NDP kinase-tubulin interactions indicates that NDP kinase does not directly charge up tubulin-GDP.

Animals↗
PubMed2006

Structural variations in the catalytic and ubiquitin-associated domains of microtubule-associated protein/microtubule affinity regulating kinase (MARK) 1 and MARK2.

The microtubule-associated protein (MAP)/microtubule affinity regulating kinase (MARK)/Par-1 phosphorylates microtubule-associated proteins tau, MAP2, and MAP4 and is involved in the regulation of microtubule-based transport. Par-1, a homologue of MARK in Drosophila and Caenorhabditis elegans, is essential for the development of embryonic polarity. Four isoforms of MARK are found in humans. Recently, we reported the crystal structure of the catalytic and ubiquitin-associated domains of MARK2, an isoform enriched in brain (Panneerselvam, S., Marx, A., Mandelkow, E.-M., and Mandelkow, E. (2006) Structure 14, 173-183). It showed that the ubiquitin-associated domain (UBA) domain has an unusual fold and binds to the N-terminal lobe of the catalytic domain. This is at variance with a previous low resolution structure derived from small angle solution scattering (Jaleel, M., Villa, F., Deak, M., Toth, R., Prescott, A. R., Van Aalten, D. M., and Alessi, D. R. (2006) Biochem. J. 394, 545-555), which predicts binding of the UBA domain to the larger, C-terminal lobe. Here we report the crystal structure of the catalytic and UBA domain of another isoform, MARK1. Although the crystal packing of the two isoforms are unrelated, the overall conformations of the molecules are similar. Notably, the UBA domain has the same unusual conformation as in MARK2, and it binds at the same site. Remarkable differences occur in the catalytic domain at helix C, the catalytic loop, and the activation segment.

Amino Acid Sequence↗
PubMed1991

Specific association of an M-phase kinase with isolated mitotic spindles and identification of two of its substrates as MAP4 and MAP1B.

Isolated mammalian (Chinese hamster ovary [CHO]) metaphase spindles were found to be enriched in a histone H1 kinase whose activity was mitotic-cycle dependent. Two substrates for the kinase were identified as MAP1B and MAP4. Partially purified spindle kinase retained activity for the spindle microtubule-associated proteins (MAPs) as well as brain and other tissue culture MAPs; on phosphorylation, spindle MAPs exhibited increased immunoreactivity with MPM-2, a monoclonal antibody specific for a subset of mitotic phosphoproteins. Immunofluorescence using an anti-thiophosphoprotein antibody localized in vitro phosphorylated spindle proteins to microtubule fibers, centrosomes, kinetochores, and midbodies. The fractionated spindle kinase was reactive with anti-human p34cdc2 antibodies and with an anti-human cyclin B but not an anti-human cyclin A antibody. We conclude that spindle MAPs undergo mitotic cycle-dependent phosphorylations in vivo and associate with a kinase that remains active on spindle isolation and may be related to p34cdc2.

Animals↗
PubMed2005

Developmentally induced changes in transcriptional program alter spatial organization across chromosomes.

Although the spatial location of genes within the nucleus has been implicated in their transcriptional status, little is known about the dynamics of gene location that accompany large-scale changes in gene expression. The mating of haploid yeast Saccharomyces cerevisiae is accompanied by a large-scale change in transcription and developmental program. We examined changes in nuclear organization that accompany stimulus by the mating pheromone alpha factor and found that most alpha-factor-induced genes become associated with components of the nuclear envelope. The myosin-like protein Mlp1, which has been implicated in mRNA export, was further shown to exhibit RNA dependence in its association with alpha-factor-induced genes. High-resolution mapping of association of chromosome III with Mlp1 revealed alpha-factor-dependent determinants of nuclear pore association, including origins of replication, specific intergenic regions, and the 3' ends of transcriptionally activated genes. Taken together, these results reveal RNA- and DNA-dependent determinants of nuclear organization as well as a detailed picture of how an entire chromosome alters its spatial conformation in response to a developmental cue.

Chromosomes, Fungal↗