Nucleohyaloplasm
Template:Mergeto Nucleohyaloplasm is the cytosol within the nucleus, without the microfilaments and the microtubules. This liquid part contains enzymes and intermediate metabolites. Many substances such as nucleotides (necessary for purposes such as the replication of DNA and production of mRNA) and enzymes (which direct activities that take place in the nucleus) are dissolved in the nucleohyaloplasm.
As a cytosol, it consists mostly of water, dissolved ions, small molecules, and large water-soluble molecules (such as protein). It contains about 20% to 30% protein. It has a high concentration of K⁺ ions and a low concentration of Na⁺ ions.
Small particles
Small particles (< 30 kDa) are able to pass through the nuclear pore complex by passive transport. The average mass range for amino acids: 75 - 204 Da. By comparison a water molecule is 18 Da. Nucleotides range in size from 176 Da (OMP) to 523 Da (GTP). The lateral speed of biological molecules in passive diffusion in water is on the order of 500 - 50 nm/sec. But in cytosol such as the nucleohyaloplasm: ~120 - 10 nm/sec due to crowding and collisions with large molecules.
Large particles
Larger particles are also able to pass through the large diameter of a nuclear pore but at almost negligible rates.[1]
A- and B-type lamins, which form separate, but interacting, stable meshworks in the lamina, have different mobilities.[2]
Structures
Of the structures local to the nucleohyaloplasm, some serve to confine it such as the inner membrane of the nuclear envelope. While others are completely suspended within it, for example, the nucleolus. Still others such as the nuclear matrix[3][4] and nuclear lamina are found throughout the inside of the nucleus.
Lamins within the nucleohyaloplasm form another regular structure the nucleoplasmic veil[5]. The veil is excluded from the nucleolus and is present during interphase.[6] The lamin structures that make up the veil bind chromatin and disrupting their structure inhibits transcription of protein-coding genes.[7] Changes also occur in the mesh size.[2]
References
- ↑ Campbell, Neil A. (1987). Biology. p. 795. ISBN 0-8053-1840-2.
- ↑ 2.0 2.1 Shimi T, Pfleghaar K, Kojima S, Pack CG, Solovei I, Goldman AE, Adam SA, Shumaker DK, Kinjo M, Cremer T, Goldman RD (2008). "The A- and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription". Genes Dev. 22 (24): 3409–21. PMID 19141474. Unknown parameter
|month=ignored (help) - ↑ Nickerson J (2001). "Experimental observations of a nuclear matrix". J. Cell. Sci. 114 (Pt 3): 463–74. PMID 11171316. Unknown parameter
|month=ignored (help) - ↑ Tetko IV, Haberer G, Rudd S, Meyers B, Mewes HW, Mayer KF (2006). "Spatiotemporal expression control correlates with intragenic scaffold matrix attachment regions (S/MARs) in Arabidopsis thaliana". PLoS Comput. Biol. 2 (3): e21. doi:10.1371/journal.pcbi.0020021. PMC 1420657. PMID 16604187. Unknown parameter
|month=ignored (help) - ↑ Goldman R, Gruenbaum Y, Moir R, Shumaker D, Spann T (2002). "Nuclear lamins: building blocks of nuclear architecture". Genes Dev. 16 (5): 533–547. doi:10.1101/gad.960502. PMID 11877373.
- ↑ Moir RD, Yoona M, Khuona S, Goldman RD. (2000). "Nuclear Lamins A and B1: Different Pathways of Assembly during Nuclear Envelope Formation in Living Cells". Journal of Cell Biology. 151 (6): 1155–1168. doi:10.1083/jcb.151.6.1155. PMID 11121432.
- ↑ Spann TP, Goldman AE, Wang C, Huang S, Goldman RD. (2002). "Alteration of nuclear lamin organization inhibits RNA polymerase II–dependent transcription". Journal of Cell Biology. 156 (4): 603–608. doi:10.1083/jcb.200112047. PMID 11854306.
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