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  • XVI.A.2.g. PSI-L
  • Sequences of PSI-L
  • Sequence Similarity Search for PSI-L

    XVI.A.2.g. PSI-L

    In barley, spinach, and Anabaena species, the PSI-L polypeptide is N-terminally blocked to amino acid sequencing (for a general review see Andersen and Scheller, 1993). In barley the apparent Molecular mass of the PSI-L polypeptide is 14 kDa, whereas the calculated mass is about 18 kDa.

    The basic structure of the PSI-L polypeptide consists of two membrane-spanning hydrophobic domains connected via a positively charged hydrophilic segment which most likely protrudes into the chloroplast lumen. The PSI-L polypeptide is very tightly bound to CPI, and is not dissociated by chaotropes.

    A query for psaL addressed to the various protein databases listed in the Biology Workbench, yielded 62 records which are depicted under Sequenced PSI-L. These sequences can be used for Sequence Similarity Searches or other manipulations using one of several routines described in the Biology Workbench or elsewhere (see AntheproW which can be downloaded via anonymous ftp from: ibcp.fr; pub/Antheprot/Windows/anthe 3_1 directory). For example a Blast Sequence Similarity Search of cucumber PSI-L addressed to the Biology Workbench (SwissProt database) is depicted below.

    Sequences of PSI-L

    Click on Sequences to view the sequences of PSI-L retrieved from various protein sequence databases by the Biology Workbench.

    Sequence Similarity Search for PSI-L

    Click on Sequence Similarity Search to view the Blast sequence similarity search results of cucumber PSI-L from the Biology workbench (SwissProt database).

    References

    1. Andersen, B. and H. V. Scheller (1993). Structure, Function and Assembly of photosystem I. In: Pigment-Protein Complexes In Plastids: Synthesis and Assembly . C. Sundqvist and M. Ryberg, (eds.), p 383-417, Academic Press, New York.

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