Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of cDNA clones encoding the complete precursor for subunit delta of thylakoid-located ATP synthase from spinach (1988)
    Springer
    Plant molecular biology 10 (1988), S. 323-330 
    Details
    ISSN: 1573-5028
    Keywords: chloroplast ATP synthase ; subunit delta ; cDNA nucleotide sequence ; transit peptide ; spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nucleotide sequence of the entire nuclear-encoded precursor for subunit delta of the ATP synthase from spinach thylakoid membranes was determined by cDNA sequencing. Appropriate recombinant DNAs were selected from pBR322 and lambda gt11 libraries made from polyadenylated RNA of greening spinach seedlings. The mature protein consists of 187 amino acid residues corresponding to a molecular weight of 20468. The precursor protein (257 amino acid residues; M r=27676) is probably processed between a Met-Val bond. The predicted secondary structure of the transit sequence (70 residues; 7.2 kDa) resembles that of the Rieske Fe/S polypeptide, but shows little similarity with those of stromal or luminal proteins. The comparison of the chloroplast delta amino acid sequence with the published delta sequences from respiratory ATP synthases of bacterial and mitochondrial sources and from the thylakoid ATP synthase of the cyanobacterium Synechococcus suggests substantial divergence at the genic level although structural elements appear to be remarkably conserved.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00029882
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    The complete amino-acid sequence of the rieske FeS-precursor protein from spinach chloroplasts deduced from cDNA analysis (1987)
    Springer
    Molecular genetics and genomics 210 (1987), S. 171-177 
    Details
    ISSN: 1617-4623
    Keywords: Photosynthesis ; Rieske iron-sulfur precursor protein ; cDNA nucleotide sequence ; Transit peptide ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Summary Several cDNA clones encoding the entire Rieske FeS-precursor protein of the chloroplast cytochrome b 6 f-complex have been isolated by high density plaque immunoscreening of a phage lambda gt11 cDNA expression library, made from poly A+-RNA of spinach seedlings. The identity of the cDNAs has been confirmed by N-terminal amino acid sequencing of the purified protein. The nucleotide sequence indicates a protein of 247 amino acid residues including a putative transit sequence of 68 amino acids corresponding to molecular masses of 26.3 kDa (precursor) and 18.8 kDa (mature protein; 179 amino acid residues). Alignteins of the sequence with sequences from Rieske FeS-proteins of respiratory electron transport chains, two of bacterial and three of mitochondrial origin, shows little sequence homology, but remarkable similarity in secondary structure including a putative N-terminal transmembrane segment of about 25 residues and the peptides CTHLGCV and CPCHGS in the C-terminal region of the protein that are involved in the binding of the Fe2S2-cluster.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00337775
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of cDNA clones encoding the complete “33 kDa” precursor protein associated with the photosynthetic oxygen-evolving complex from spinach (1987)
    Springer
    Molecular genetics and genomics 207 (1987), S. 288-293 
    Details
    ISSN: 1617-4623
    Keywords: Photosynthetic oxygen evolution ; “33 kDa” protein ; cDNA nucleotide sequence ; Transit peptide ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Several cDNA clones encoding the “33 kDa” protein associated with the photosynthetic water oxidation activity of spinach were sequenced. A 1208 bp insert of one of the clones encodes the entire 331 amino acid residues of the precursor protein including 84 amino acids (8.5 kDa) of the amino-terminal transit peptide, 49 bp of the 5′ and 111 bp of the 3′ untranslated segment of the mRNA. The 3′ poly(A) tail starts 19 bp downstream from a putative polyadenylation signal, TATAAA. The hydrophilic mature protein consists of 247 amino acid residues corresponding to an Mr of 26.5 kDa, which is 6.5 kDa smaller than the value determined by SDS-polyacrylamide gel electrophoresis (33–34 kDa), and shows a certain degree of conservation with the putative Mn-complexing active sites of bacterial Mn-dependent superoxide dismutases. The anatomy of the unusually long transit sequence is discussed with regard to current concepts of protein import into and protein routein within the organelle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331591
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...