Words similar to subunits
Example sentences for: subunits
How can you use “subunits” in a sentence? Here are some example sentences to help you improve your vocabulary:
The T. acidophilum intein shows significant sequence similarity to the inteins found in the A-ATPase catalytic subunits of Pyrococcus.
Overall, these data are consistent with previous reports that endocrine cells express voltage-sensitive ion channels that can contribute to the regulation of not only resting membrane potential and cell volume, but also cell proliferation and steroidogenesis [ 12 13 16 18 21 28 29 30 31 32 33 34 35 36 37 ] . The K +currents blocked by 4-AP in pig GC are conducted by ion channels formed by heteromeric complexes of pore-forming subunits from the KCNA (also called Kv1 or Shaker) family of proteins and accessory subunits from the KCNAB (also called Kvβ) family of proteins [ 4 ] . Similar 4-AP-sensitive K +currents play a key role in transduction of mitogenic signals in a variety of cell types, and 4-AP treatment has been associated with not only growth arrest but also apoptosis [ 2 3 8 9 10 14 38 39 40 41 42 ] .
The PRC-H subunits and their close relatives from cyanobacteria, non-photosynthetic α-proteobacteria and D. radiodurans form the first of these groups.
The initial step of the insertion can proceed in the presence of either Mg.ATP or a non-hydrolyzable ATP-analog and involves oligomerization of the BchD and BchI subunits to form an oligomeric ring of AAA protomers that resembles the ring structure of NSF and other AAA proteins [ 14 32 ] . The second step of the insertion involves an obligatory hydrolysis of ATP that is tightly coupled with the transfer of the chelated Mg 2+to the protoporphyrin ring by BchH [ 49 ] . Although the details differ from midasin, particularly with respect to the subunit composition of the AAA ring, this chelation reaction provides a structural model suggesting that the function of the midasin M-domain may be to regulate the ATPase activity of the AAA protomers in the pseudo-hexameric ring and thus couple ATP hydrolysis to the binding of a protein ligand at the MIDAS site.
Both the spatial arrangement of the ASCR domain in the β' subunits and its extreme sequence divergence with respect to the ASCR domains of the α-subunit suggests that it has acquired a new function.
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