The Role of Specific Amino Acid Residues in The Vibrational Properties of Plastocyanin

2002 ◽  
Vol 106 (40) ◽  
pp. 10474-10481 ◽  
Author(s):  
E. Fraga ◽  
G. R. Loppnow
Keyword(s):  
Amino Acid ◽  
Vibrational Properties ◽  
Amino Acid Residues ◽  
Specific Amino Acid

scholarly journals Analysis of Mason-Pfizer Monkey Virus Gag Domains Required for Capsid Assembly in Bacteria: Role of the N-Terminal Proline Residue of CA in Directing Particle Shape

2000 ◽  
Vol 74 (18) ◽  
pp. 8452-8459 ◽  
Author(s):  
Michaela Rumlova-Klikova ◽  
Eric Hunter ◽  
Milan V. Nermut ◽  
Iva Pichova ◽  
Tomas Ruml
Keyword(s):  
Amino Acid ◽  
Nucleocapsid Protein ◽  
Mammalian Cells ◽  
Matrix Protein ◽  
Amino Acid Residues ◽  
Membrane Expression ◽  
Specific Amino Acid ◽  
Plasma Membrane Expression ◽  
C And N

ABSTRACT Mason-Pfizer monkey virus (M-PMV) preassembles immature capsids in the cytoplasm prior to transporting them to the plasma membrane. Expression of the M-PMV Gag precursor in bacteria results in the assembly of capsids indistinguishable from those assembled in mammalian cells. We have used this system to investigate the structural requirements for the assembly of Gag precursors into procapsids. A series of C- and N-terminal deletion mutants progressively lacking each of the mature Gag domains (matrix protein [MA]-pp24/16-p12-capsid protein [CA]-nucleocapsid protein [NC]-p4) were constructed and expressed in bacteria. The results demonstrate that both the CA and the NC domains are necessary for the assembly of macromolecular arrays (sheets) but that amino acid residues at the N terminus of CA define the assembly of spherical capsids. The role of these N-terminal domains is not based on a specific amino acid sequence, since both MA-CA-NC and p12-CA-NC polyproteins efficiently assemble into capsids. Residues N terminal of CA appear to prevent a conformational change in which the N-terminal proline plays a key role, since the expression of a CA-NC protein lacking this proline results in the assembly of spherical capsids in place of the sheets assembled by the CA-NC protein.

Role of Specific Amino Acid Residues in T4 Endonuclease V That Alter Nontarget DNA Binding†

Biochemistry ◽  
1997 ◽  
Vol 36 (14) ◽  
pp. 4080-4088 ◽  
Author(s):  
Simon G. Nyaga ◽  
M. L. Dodson ◽  
R. Stephen Lloyd
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Amino Acid Residues ◽  
Specific Amino Acid ◽  
Endonuclease V

scholarly journals Role of KLHL3 and dietary K+ in regulating KS-WNK1 expression

2021 ◽  
Author(s):  
Mauricio Ostrosky-Frid ◽  
Maria Chavez-Canales ◽  
Jinwei Zhang ◽  
Olena Andrukova ◽  
Eduardo R. Argaiz ◽  
...  
Keyword(s):  
Amino Acid ◽  
Physiological Role ◽  
Kinase Domain ◽  
Severe Form ◽  
Missense Mutations ◽  
Amino Acid Residues ◽  
Specific Amino Acid ◽  
And Function ◽  
Familial Hyperkalemic Hypertension

The physiological role of the shorter isoform of WNK1 that is exclusively expressed in the kidney (KS-WNK1), with particular abundance in the distal convoluted tubule, remains elusive. KS-WNK1 despite lacking the kinase domain, is nevertheless capable of stimulating the NaCl cotransporter (NCC), apparently through activation of WNK4. It has recently been shown that a less severe form of the Familial Hyperkalemic Hypertension featuring only hyperkalemia is caused by missense mutations in the WNK1 acidic domain that preferentially affect CUL3-KLHL3 E3-induced degradation of KS-WNK1, rather than that of the full-length WNK1 (L-WNK1). Here we show that L-WNK1 is indeed less impacted by the CUL3-KLHL3 E3 ligase complex compared to KS-WNK1. We demonstrate that the unique 30 amino acid amino N-terminal fragment of KS-WNK1 is essential for its activating effect on NCC and recognition by KLHL3. We identify specific amino acid residues in this region critical for the functional effect of KS-WNK1 and KLHL3 sensitivity. To further explore this, we generated KLHL3-R528H knock-in mice that mimic human mutations causing Familial Hyperkalemic Hypertension. These mice revealed that the KLHL3 mutation specifically increased expression of KS-WNK1 in the kidney. We also observed that in wild type mice, expression of KS-WNK1 is only detectable after exposure to low potassium diet. These findings provide new insights into the regulation and function of KS-WNK1 by the CUL3-KLHL3 complex in DCT and indicate that this pathway is regulated by dietary K+ levels.

scholarly journals Deletion of the Actin-Associated Tropomyosin Tpm3 Leads to Reduced Cell Complexity in Cultured Hippocampal Neurons—New Insights into the Role of the C-Terminal Region of Tpm3.1

Cells ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 715
Author(s):  
Tamara Tomanić ◽  
Claire Martin ◽  
Holly Stefen ◽  
Esmeralda Parić ◽  
Peter Gunning ◽  
...  
Keyword(s):  
Amino Acid ◽  
Hippocampal Neurons ◽  
Molecular Mechanisms ◽  
Growth Cones ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
C Terminus ◽  
Primary Mouse ◽  
Terminal Amino

Tropomyosins (Tpms) have been described as master regulators of actin, with Tpm3 products shown to be involved in early developmental processes, and the Tpm3 isoform Tpm3.1 controlling changes in the size of neuronal growth cones and neurite growth. Here, we used primary mouse hippocampal neurons of C57/Bl6 wild type and Bl6Tpm3flox transgenic mice to carry out morphometric analyses in response to the absence of Tpm3 products, as well as to investigate the effect of C-terminal truncation on the ability of Tpm3.1 to modulate neuronal morphogenesis. We found that the knock-out of Tpm3 leads to decreased neurite length and complexity, and that the deletion of two amino acid residues at the C-terminus of Tpm3.1 leads to more detrimental changes in neurite morphology than the deletion of six amino acid residues. We also found that Tpm3.1 that lacks the 6 C-terminal amino acid residues does not associate with stress fibres, does not segregate to the tips of neurites, and does not impact the amount of the filamentous actin pool at the axonal growth cones, as opposed to Tpm3.1, which lacks the two C-terminal amino acid residues. Our study provides further insight into the role of both Tpm3 products and the C-terminus of Tpm3.1, and it forms the basis for future studies that aim to identify the molecular mechanisms underlying Tpm3.1 targeting to different subcellular compartments.

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