Limits...
The Origin and Evolution of the Plant Cell Surface: Algal Integrin-Associated Proteins and a New Family of Integrin-Like Cytoskeleton-ECM Linker Proteins.

Becker B, Doan JM, Wustman B, Carpenter EJ, Chen L, Zhang Y, Wong GK, Melkonian M - Genome Biol Evol (2015)

Bottom Line: The extracellular matrix of scaly green flagellates consists of small organic scales consisting of polysaccharides and scale-associated proteins (SAPs).Gralins are absent from embryophytes.A model for the evolution of the cell surface proteins in Plantae is discussed.

View Article: PubMed Central - PubMed

Affiliation: Biozentrum Köln, Botanical Institute, Universität zu Köln, Germany b.becker@uni-koeln.de.

Show MeSH

Related in: MedlinePlus

Cloning strategy of SAP98 and domain structure of SAP98, SAP116, and SAP126 from Scherffelia dubia. (A) Isolation of a small PCR fragment, containing the sequence information for a 14 aa peptide from SAP98. The peptide sequence, the corresponding degenerated nucleotide sequence, and the sequences of five clones are given. New sequence information is in bold and the primer region is in italics. (B) Extension of the short peptide sequence using inverse PCR (gray) and 3’-RACE (white), and database searches (1KP project, black). The position of peptide sequence obtained by mass spectrometry is given. (C–E) Domain structure of SAP98 (C), SAP116 (D), and SAP126 (E). The aa sequence of the N-terminal ends including the SP and the TMD is also given. Note: The N-terminal sequence of SAP126 (gray) is from the most similar sequence from Tetraselmis striata.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4494055&req=5

evv089-F1: Cloning strategy of SAP98 and domain structure of SAP98, SAP116, and SAP126 from Scherffelia dubia. (A) Isolation of a small PCR fragment, containing the sequence information for a 14 aa peptide from SAP98. The peptide sequence, the corresponding degenerated nucleotide sequence, and the sequences of five clones are given. New sequence information is in bold and the primer region is in italics. (B) Extension of the short peptide sequence using inverse PCR (gray) and 3’-RACE (white), and database searches (1KP project, black). The position of peptide sequence obtained by mass spectrometry is given. (C–E) Domain structure of SAP98 (C), SAP116 (D), and SAP126 (E). The aa sequence of the N-terminal ends including the SP and the TMD is also given. Note: The N-terminal sequence of SAP126 (gray) is from the most similar sequence from Tetraselmis striata.

Mentions: SAPs were isolated by 2D-gel electrophoresis (under non-reducing/reducing conditions) as described by Becker et al. (1996). SAPs were sequenced by mass spectrometry. Sequences of several peptides were obtained for each of four different SAPs (supplementary table S1, Supplementary Material online). Database searches (NCBI proteins and expressed sequence tags [ESTs]) failed to identify any protein showing similarity to more than a single SAP peptide in its sequence. Standard PCR using degenerate forward and reverse primers for each peptide also failed to isolate cDNA or genomic fragments coding for any SAP. However, amplification of a short fragment of known length representing a single peptide using short oligonucleotide primers was successful in a single case for a SAP98 peptide (fig. 1A).Fig. 1.—


The Origin and Evolution of the Plant Cell Surface: Algal Integrin-Associated Proteins and a New Family of Integrin-Like Cytoskeleton-ECM Linker Proteins.

Becker B, Doan JM, Wustman B, Carpenter EJ, Chen L, Zhang Y, Wong GK, Melkonian M - Genome Biol Evol (2015)

Cloning strategy of SAP98 and domain structure of SAP98, SAP116, and SAP126 from Scherffelia dubia. (A) Isolation of a small PCR fragment, containing the sequence information for a 14 aa peptide from SAP98. The peptide sequence, the corresponding degenerated nucleotide sequence, and the sequences of five clones are given. New sequence information is in bold and the primer region is in italics. (B) Extension of the short peptide sequence using inverse PCR (gray) and 3’-RACE (white), and database searches (1KP project, black). The position of peptide sequence obtained by mass spectrometry is given. (C–E) Domain structure of SAP98 (C), SAP116 (D), and SAP126 (E). The aa sequence of the N-terminal ends including the SP and the TMD is also given. Note: The N-terminal sequence of SAP126 (gray) is from the most similar sequence from Tetraselmis striata.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4494055&req=5

evv089-F1: Cloning strategy of SAP98 and domain structure of SAP98, SAP116, and SAP126 from Scherffelia dubia. (A) Isolation of a small PCR fragment, containing the sequence information for a 14 aa peptide from SAP98. The peptide sequence, the corresponding degenerated nucleotide sequence, and the sequences of five clones are given. New sequence information is in bold and the primer region is in italics. (B) Extension of the short peptide sequence using inverse PCR (gray) and 3’-RACE (white), and database searches (1KP project, black). The position of peptide sequence obtained by mass spectrometry is given. (C–E) Domain structure of SAP98 (C), SAP116 (D), and SAP126 (E). The aa sequence of the N-terminal ends including the SP and the TMD is also given. Note: The N-terminal sequence of SAP126 (gray) is from the most similar sequence from Tetraselmis striata.
Mentions: SAPs were isolated by 2D-gel electrophoresis (under non-reducing/reducing conditions) as described by Becker et al. (1996). SAPs were sequenced by mass spectrometry. Sequences of several peptides were obtained for each of four different SAPs (supplementary table S1, Supplementary Material online). Database searches (NCBI proteins and expressed sequence tags [ESTs]) failed to identify any protein showing similarity to more than a single SAP peptide in its sequence. Standard PCR using degenerate forward and reverse primers for each peptide also failed to isolate cDNA or genomic fragments coding for any SAP. However, amplification of a short fragment of known length representing a single peptide using short oligonucleotide primers was successful in a single case for a SAP98 peptide (fig. 1A).Fig. 1.—

Bottom Line: The extracellular matrix of scaly green flagellates consists of small organic scales consisting of polysaccharides and scale-associated proteins (SAPs).Gralins are absent from embryophytes.A model for the evolution of the cell surface proteins in Plantae is discussed.

View Article: PubMed Central - PubMed

Affiliation: Biozentrum Köln, Botanical Institute, Universität zu Köln, Germany b.becker@uni-koeln.de.

Show MeSH
Related in: MedlinePlus